Sugar transport by the bacterial phosphotransferase system. Characterization of the sulfhydryl groups and site-specific labeling of enzyme I.
AuthorsHan MK, Roseman S, Brand L
JournalJ Biol Chem
PubMed ID2404975
'Enzyme I is the first protein of the phospho transfer sequence in the bacterial phosphoenolpyruvate:glycose phosphotransferase system. This protein exhibits a temperature-dependent monomer/dimer equilibrium. The nucleotide sequence of Escherichia coli ptsI indicates four -SH residues per subunit (Saffen, D. W., Presper, K. A., Doering, T. L., and Roseman, S. (1987) ... More
Arrangement of the COOH-terminal and NH2-terminal domains of caldesmon bound to actin.
AuthorsGraceffa P
JournalBiochemistry
PubMed ID9092808
'Smooth muscle caldesmon is a single polypeptide chain with its NH2- and COOH-terminal domains separated by a long alpha-helix. Caldesmon was labeled at either Cys-153 in the NH2 domain or Cys-580 in the COOH domain with a variety of fluorescence probes. Fluorescence intensity, peak position, and polarization of probes on ... More
Local conformational changes in the Vibrio Na+/galactose cotransporter.
AuthorsVeenstra M, Lanza S, Hirayama BA, Turk E, Wright EM
JournalBiochemistry
PubMed ID15035632
'Na(+) and sugar transport by cotransporters (symporters) is thought to occur as a series of ordered ligand-induced conformational changes. To localize these conformational changes in a bacterial Na(+)/galactose cotransporter, we have employed a combination of cysteine-scanning and fluorescence techniques. Single or pairs of cysteine residues were introduced into the external ... More
Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy.
AuthorsYao Y, Schöneich C, Squier TC
JournalBiochemistry
PubMed ID8011644
'Structural changes associated with the calcium-dependent activation of wheat germ calmodulin (CaM) were assessed through measurements of steady-state and time-resolved changes in the fluorescence associated with (1) the unique tyrosine (Tyr139) located in calcium binding loop IV or (2) N-(1-pyrenyl)-maleimide (PM) or 4-(iodoacetamido)salicylic acid (IASA) covalently attached to Cys27 present ... More
The in situ labeling of histone H3 in chromatin by a fluorescent probe.
AuthorsMooney D, Thompson LM, Simpkins H
JournalBiochim Biophys Acta
PubMed ID7417501
'A sulfhydryl-specific fluorescent probe, N-3-pyrene maleimide, has been shown to label with high efficiency the sulfhydryl groups of histone H3 in nonsheared chromatin. The probe labels chromatin preparations obtained by mild homogenization or nuclease treatment of rat liver and mouse thymocyte, but not chick erythrocyte nuclei. Mononucleosomes from all nuclear ... More
The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein.
AuthorsGorovits BM, Horowitz PM
JournalJ Biol Chem
PubMed ID7768899
'Steady-state fluorescence polarization was used to examine the chaperonin cpn60 that was covalently labeled with pyrene. Two compounds, 1-pyrenesulfonyl chloride or N-(1-pyrene)maleimide, were used to incorporate up to 8 mol of pyrene per mol of cpn60 14-mer. The fluorescence lifetime of the cpn60-pyrenesulfonyl chloride conjugate exhibited a double exponential decay: ... More
Conformational changes in rat liver chromatin after liver regeneration.
AuthorsSimpkins H, Thompson LM, Waldeck N, Gross DS, Mooney D
JournalBiochem J
PubMed ID7305956
'N-Pyrenemaleimide, a fluorescent probe that specifically labels histone H3 of rat liver chromatin in situ, was used to monitor the accessibility of histone H3 in chromatin isolated from rat liver at different times during degeneration. At times of maximum DNA synthesis (18--24 h after hepatectomy), the accessibility of the probe ... More
Close proximity of Cys64 and Cys140 in the delta subunit of Escherichia coli F1-ATPase.
AuthorsZiegler M, Xiao R, Penefsky HS
JournalJ Biol Chem
PubMed ID8307987
'The delta subunit of the F1-ATPase from Escherichia coli contains 2 cysteine residues, one at position 64 and the second at position 140 of the amino acid sequence. These residues were specifically labeled with sulfhydryl reagents in this study without labeling other -SH groups in the enzyme. Modification of Cys140 ... More
Structural organization of chloroplast coupling factor.
AuthorsSnyder B, Hammes GG
JournalBiochemistry
PubMed ID2859887
'Fluorescence resonance energy transfer measurements have been used to construct spatial maps for the accessible sulfhydryl of the gamma subunit (dark site) and the essential tyrosine residue of the beta subunits relative to previously mapped sites on the H+-ATPase from chloroplasts. The extent of energy transfer was measured between a ... More
Mapping sonic hedgehog-receptor interactions by steric interference.
AuthorsPepinsky RB, Rayhorn P, Day ES, Dergay A, Williams KP, Galdes A, Taylor FR, Boriack-Sjodin PA, Garber EA
JournalJ Biol Chem
PubMed ID10753901
'We have defined regions in the Sonic hedgehog (Shh) molecule that are important for Patched (Ptc) receptor binding by targeting selected surface amino acid residues with probes of diverse sizes and shapes and assessing the effects of these modifications on function. Eleven amino acid residues that surround the surface of ... More
Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease.
AuthorsLehtonen JY, Kinnunen PK
JournalBiophys J
PubMed ID9138570
'The well-characterized integral membrane protein lactose (lac) permease from Escherichia coli was reconstituted together with trace amounts (molar fraction X = 0.005 of the total phospholipid) of different pyrene-labeled phospholipid analogs into 1-palmitoyl-2-oleoyl-sn-glycero-3-sn-glycero-3-phospho-rac'-glycerol (POPG) liposomes. Effects of lac permease on bilayer lipid dynamics were investigated by measuring the excimer-to-monomer fluorescence ... More
Conformational transition of Escherichia coli RNA polymerase induced by the interaction of sigma subunit with core enzyme.
AuthorsWu FY, Yarbrough LR, Wu CW
JournalBiochemistry
PubMed ID782516
'The isolated sigma subunit of Escherichia coli RNA polymerase has been labeled covalently with a fluorescent probe, N-(1-pyrene)maleimide. The labeled sigma subunit (PM-sigma) still retained its biological activity in stimulating transcription of T7 DNA by core enzyme. When a stoichiometric amount of core enzyme was added to a solution ... More
Variable conformation and dynamics of calmodulin complexed with peptides derived from the autoinhibitory domains of target proteins.
AuthorsYao Y, Squier TC
JournalBiochemistry
PubMed ID8639633
'Calcium-saturated calmodulin (CaM) can bind and activate many target proteins through the direct association with the respective autoinhibitory domains. The CaM binding sequences within the autoinhibitory domains of these proteins have little sequence homology, and the mechanisms associated with CaM's ability to recognize and productively bind with these variable sequences ... More
'PA(63), the active 63 kDa form of anthrax protective antigen, forms a heptameric ring-shaped oligomer that is believed to represent a precursor of the membrane pore formed by this protein. When maintained at pH >/=8.0, this "prepore" dissociated to monomeric subunits upon treatment with SDS at room temperature, but treatment ... More
Pyrene excimer fluorescence: a spatially sensitive probe to monitor lipid-induced helical rearrangement of apolipophorin III.
AuthorsSahoo D, Narayanaswami V, Kay CM, Ryan RO
JournalBiochemistry
PubMed ID10828977
'Manduca sexta apolipophorin III (apoLp-III), an 18-kDa, monomeric, insect hemolymph apolipoprotein, is comprised of five amphipathic alpha-helices arranged as a globular bundle in the lipid-free state. Upon lipid binding, it is postulated that the bundle opens, exposing a continuous hydrophobic surface which becomes available for lipid interaction. To investigate lipid ... More
Reversed-phase ion-pair high-performance liquid chromatography of mercaptoacetate and N-acetylcysteine after derivatization with N-(1-pyrene)maleimide and N-(7-dimethylamino-4-methyl-3-coumarinyl)maleimide.
AuthorsKågedal B, Källberg M
JournalJ Chromatogr
PubMed ID7096475
'We have developed a high-performance liquid chromatographic system capable of resolving mercaptoacetate and N-acetylcysteine as their N-(1-pyrene)maleimide (PM) and N-(7-dimethylamino-4-methyl-3-coumarinyl)maleimide (DACM) derivatives. Good resolution was obtained by ion pairing with tetramethylammonium hydroxide and chromatography on reversed phase. The detection limits for the thiols were about 50 fmol as their DACM ... More
Interaction between cell-binding domain and extracellular matrix-binding domain of fibronectin determined by fluorescence depolarization.
AuthorsMiyamoto Y, Yokoya A, Ishizaka S
JournalBiochim Biophys Acta
PubMed ID3355842
'Interaction of domains in fibronectin was observed by photometry of fluorescence polarization of three kinds of dye; [N-(1-anilinonaphthyl-4)]maleimide (ANM tau = 5 ns), [N-(3-fluoranthyl)]maleimide (FAM tau = 20 ns), and [N-(3-pyrene)]maleimide (PRM tau = 100 ns). Each dye was labeled at a free sulfhydryl group in the cell-binding domain. Neither ... More
Identification of cysteine residues in lamb kidney (Na,K)-ATPase essential for ouabain binding.
AuthorsKirley TL, Peng M
JournalJ Biol Chem
PubMed ID1657908
'N-(1-Pyrene)maleimide is a hydrophobic, sulfhydryl-directed, chemical modification probe which, at a low concentration, inhibits the capacity of lamb kidney sodium- and potassium-activated adenosine triphosphatase [Na,K)-ATPase; EC 3.6.1.3) to bind ouabain. This inhibition is partially blocked by preincubation of the enzyme with ouabagenin, an aglycone derivative which can be used as ... More
Sugar transport by the bacterial phosphotransferase system. Fluorescence studies of subunit interactions of enzyme I.
AuthorsHan MK, Knutson JR, Roseman S, Brand L
JournalJ Biol Chem
PubMed ID2404976
'Enzyme I of the bacterial phosphoenolpyruvate:glycose phosphotransferase system (PTS) exhibits a temperature-dependent monomer/dimer equilibrium. The accompanying paper (Han, M. K., Roseman, S., and Brand, L. (1990) J. Biol. Chem. 265, 1985-1995) shows that the C-terminal -SH residue (Cys-575) can be modified specifically with fluorescent probes such as pyrene maleimide. The ... More
Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP.
AuthorsKliche W, Pfannstiel J, Tiepold M, Stoeva S, Faulstich H
JournalBiochemistry
PubMed ID10441124
'A series of thiol-specific cross-linking reagents were prepared for studying the kinetics of cross-linking between SH1 (Cys(707)) and SH2 (Cys(697)) in rabbit skeletal muscle myosin subfragment 1. The reagents were of the type RSS(CH(2))(n)()SSR, with R = 3-carboxy-4-nitrophenyl and n = 3, 6, 7, 8, 9, 10, and 12, spanning ... More
Fluorescence studies of the aged erythrocyte membranes.
AuthorsTozzi-Ciancarelli MG, D'Alfonso A, Tozzi E, Troiani-Sevi E, De Matteis G
JournalCell Mol Biol
PubMed ID2731189
'The most important purpose of this research is to characterize by means of fluorescence polarization the structural and functional changes which occur in the membrane of the human erythrocytes during aging process. Our results provide evidence of a significant increase of membrane fluidity in the deep lipid core and in ... More
Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin.
AuthorsJanmey PA, Lamb J, Allen PG, Matsudaira PT
JournalJ Biol Chem
PubMed ID1318302
'The polyphosphoinositides phosphatidylinositol 4-monophosphate (PIP) and phosphatidylinositol 4,5-bisphosphate (PIP2) inactivate the actin filament-severing proteins villin and gelsolin and dissociate them from monomeric and polymeric actin. A potential polyphosphoinositide- (PPI) binding site of human plasma gelsolin regulating filament severing has been localized to the region between residues 150-169 and to the ... More
Excimer fluorescence of pyrene-tropomyosin adducts.
AuthorsLin TI
JournalBiophys Chem
PubMed ID7115884
'Studies of the fluorescence of N-(1-pyrene)maleimide and N-(1-pyrenyl)iodoacetamide adducts of rabbit skeletal muscle tropomyosin revealed the presence of excimer fluorescence characterized by a broad emission band at 480 nm with a shoulder at 505 nm. Monomer fluorescence decay exhibited different lifetimes, viz., about 3, 22 and 87 ns for the ... More
Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 1. Spatial disposition of cysteine residues in the gamma subunit analyzed by fluorescence-quenching and energy-transfer measurements.
AuthorsNarayanaswami V, Kim J, McNamee MG
JournalBiochemistry
PubMed ID8241131
'The nicotinic acetylcholine receptor from Torpedo californica was labeled with a fluorescent, lipophilic probe, N-(1-pyrenyl)maleimide, specific for sulfhydryls in a hydrophobic environment, and was found to alkylate Cys 416, Cys 420 and Cys 451 in the gamma subunit [Li, L., Schuchard, M., Palma, A., Pradier, L., & McNamee, M.G. (1990) ... More
A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.
AuthorsWest JM, Tsuruta H, Kantrowitz ER
JournalJ Biol Chem
PubMed ID14581486
'A new system has been developed capable of monitoring conformational changes of the 240s loop of aspartate transcarbamoylase, which are tightly correlated with the quaternary structural transition, with high sensitivity in solution. Pyrene, a fluorescent probe, was conjugated to residue 241 in the 240s loop of aspartate transcarbamoylase to monitor ... More
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
'Cpn60 was labeled with pyrene maleimide in order to follow structural rearrangements in the protein triggered by the binding of nucleotides and cpn10. The conjugate binds ATP, AMP-PNP, and ADP(P(i)) with pyrene fluorescence enhancements of 60%, 60%, and 15%, respectively. In each case, binding is cooperative with half-saturation (K1/2) occurring ... More
Relaxation time, interthiol distance, and mechanism of action of ribosomal protein S1.
AuthorsOdom OW, Deng HY, Subramanian AR, Hardesty B
JournalArch Biochem Biophys
PubMed ID6201138
'The two sulfhydryl groups of ribosomal protein S1 from Escherichia coli have been labeled with fluorescent maleimides and the distance between them has been determined by nonradiative energy transfer. This distance was found to be approximately 27 A for both free S1 and S1 bound to 30 S subunits. This ... More
Interaction of the catalytic subunits of protein phosphatase-1 and 2A with inhibitor-1 and 2: a fluorescent study with sulfhydryl-specific pyrene maleimide.
AuthorsCsortos C, Matkó J, Erdödi F, Gergely P
JournalBiochem Biophys Res Commun
PubMed ID2162668
'The catalytic subunits of protein phosphatase-1 and 2A were covalently modified in their reactive sulfhydryl groups with N-(3-Pyrene) maleimide resulting in fluorescent labeling of the proteins to an extent of 0.85 and 0.9 mole dye/mole enzyme, respectively. The reaction of the sulfhydryl group led to the partial inactivation of both ... More
Tropomyosin-troponin regulation of actin does not involve subdomain 2 motions.
AuthorsGerson JH, Kim E, Muhlrad A, Reisler E
JournalJ Biol Chem
PubMed ID11278830
'Dynamic properties of F-actin structure prompted suggestions (Squire, J. M., and Morris, E. P. (1998) FASEB J. 12, 761-771) that actin subdomain 2 movements play a role in thin-filament regulation. Using fluorescently labeled yeast actin mutants Q41C, Q41C/C374S, and D51C/C374S and azidonitrophenyl putrescine (ANP) Gln(41)-labeled alpha-actin, we monitored regulation-linked changes ... More
Fluorophores at the N terminus of nascent chloramphenicol acetyltransferase peptides affect translation and movement through the ribosome.
AuthorsRamachandiran V, Willms C, Kramer G, Hardesty B
JournalJ Biol Chem
PubMed ID10636875
'Structurally different fluorescent probes were covalently attached to methionyl-tRNA(f) and tested for their incorporation into nascent peptides and full-length protein using an Escherichia coli cell-free coupled transcription/translation system. Bovine rhodanese and bacterial chloramphenicol acetyltransferase (CAT) were synthesized using derivatives of cascade yellow, eosin, pyrene, or coumarin attached to [(35)S]Met-tRNA(f). All ... More
Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer.
AuthorsRao A, Martin P, Reithmeier RA, Cantley LC
JournalBiochemistry
PubMed ID497152
'The stilbenedisulfonate inhibitory site of the human erythrocyte anion-exchange system has been characterized by using serveral fluorescent stilbenedisulfonates. The covalent inhibitor 4-benzamido-4''-isothiocyanostilbene-2,2''-disulfonate (BIDS) reacts specifically with the band 3 protein of the plasma membrane when added to intact erythrocytes, and the reversible inhibitors 4,4''-dibenzamidostilbene-2,2''-disulfonate (DBDS) and 4-benzamido-4''-aminostilbene-2,2''-disulfonate (BADS) show a ... More
Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles.
AuthorsXian W, Vegners R, Janmey PA, Braunlin WH
JournalBiophys J
PubMed ID8599675
'The peptide G(150-169) corresponds to a phosphatidylinositol 4,5-bisphosphate (PIP2) and filamentous actin (F-actin) binding site on gelsolin (residues 150-169, with the sequence KHVVPNEVVVQRLFQVKGRR). The conformation of this peptide in trifluoroethanol (TFE) aqueous solution was determined by 1H nuclear magnetic resonance as the first step toward understanding the structural aspects of ... More
The rate of polymerization of rabbit skeletal muscle actin is enhanced by polyethylene glycol.
AuthorsStrömqvist M, Backman L, Shanbhag VP
JournalJ Muscle Res Cell Motil
PubMed ID6480818
'The effect of polyethylene glycol on the kinetics of actin polymerization was determined by monitoring the enhancement in the fluorescence of pyrenyl-labelled actin. The polymerization of actin at 15 mM KCl was in addition followed by viscometry and light scattering. All three methods showed that the overall rate of polymerization ... More
Loss of conformational stability in calmodulin upon methionine oxidation.
AuthorsGao J, Yin DH, Yao Y, Sun H, Qin Z, Schöneich C, Williams TD, Squier TC
JournalBiophys J
PubMed ID9512014
'We have used electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and fluorescence spectroscopy to investigate the secondary and tertiary structural consequences that result from oxidative modification of methionine residues in wheat germ calmodulin (CaM), and prevent activation of the plasma membrane Ca-ATPase. Using ESI-MS, we have measured rates of ... More
Labeling of functionally sensitive sulfhydryl-containing domains of acetylcholine receptor from Torpedo californica membranes.
AuthorsClarke JH, Martinez-Carrion M
JournalJ Biol Chem
PubMed ID3733702
'N-(1-Pyrene)maleimide, a fluorescent, lipophilic, alkylating agent, was used as a probe for the nicotinic acetylcholine receptor (AChR). Preincubation with N-(1-pyrene)maleimide under nonreducing conditions inhibits agonist-induced cation permeability of AChR-enriched membranes. This inhibition is dependent on the concentration of N-(1-pyrene)maleimide used. This correlation was also exhibited by resonance energy transfer of ... More
A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase.
AuthorsBhattacharyya T, Roy S
JournalBiochemistry
PubMed ID8369295
'Glutaminyl-tRNA synthetase from Escherichia coli is a member of a subgroup of aminoacyl-tRNA synthetases that do not catalyze ATP-PPi exchange in the absence of the cognate tRNA. Such behavior suggests conformational changes upon substrate binding. Two different fluorescent probes, pyrenylmaleimide and acrylodan, were used to specifically label a nonessential sulfhydryl ... More
Specific fluorescent labeling of alpha 2-macroglobulin-bound proteases: accessibility and localization of their active site within the complex.
AuthorsTourbez M, Pochon F
JournalBiochimie
PubMed ID2430627
'Pyrenebutylmethylphosphonofluoridate reacts with trypsin and elastase to yield a conjugate with a stoichiometry of one fluorescent label per enzyme molecule as already observed with chymotrypsin. The kinetics of inactivation indicate that the serine active center of the proteases is involved in the labeling reaction. The binding of the proteases to ... More
Use of site-directed fluorescence labeling to study proximity relationships in the lactose permease of Escherichia coli.
AuthorsJung K, Jung H, Wu J, Privé GG, Kaback HR
JournalBiochemistry
PubMed ID8241112
'The lactose permease of Escherichia coli is a paradigm for polytopic membrane transport proteins that transduce free energy stored in an electrochemical ion gradient into work in the form of a concentration gradient. Although the permease consists of 12 hydrophobic transmembrane domains in probable alpha-helical conformation that traverse the membrane ... More
The plasma membrane H+-ATPase of Neurospora crassa. Properties of two reactive sulfhydryl groups.
AuthorsDavenport JW, Slayman CW
JournalJ Biol Chem
PubMed ID2903147
'Previous work with N-ethylmaleimide (NEM) has defined two sites on the Neurospora plasma membrane H+-ATPase. Modification of one (the "fast" site) by NEM is rapid but does not affect ATPase activity, while modification of the other (the "slow" site) inactivates the enzyme and is protectable by MgATP or MgADP. In ... More
Nucleosome core particle self-assembly kinetics and stability at physiological ionic strength.
AuthorsDiaz P, Daban JR
JournalBiochemistry
PubMed ID3801441
'Micrococcal nuclease, DNase I, and trypsin have been employed to study the kinetics of core particle self-assembly by salt jump from 2.0 to 0.2 M NaCl. A few seconds after the initiation of the reassociation reaction, the bulk of core particle DNA becomes protected from digestion by micrococcal nuclease, whereas ... More
Comparative study of the kinetic and structural properties of monomeric and oligomeric forms of sarcoplasmic reticulum ATPase.
AuthorsYamamoto T, Yantorno RE, Tonomura Y
JournalJ Biochem (Tokyo)
PubMed ID6147342
'Sarcoplasmic reticulum (SR) isolated from rabbit muscle was treated with N-ethyl-maleimide (NEM) to specifically inhibit the dephosphorylation step of the Ca2+,Mg2+-dependent ATPase reaction. However, when this membrane was solubilized with dodecyl octaethyleneglycol monoether (C12E8), rapid decomposition of the phosphoenzyme (EP) was observed both in the absence and presence of Mg2+. ... More
The mitochondrial oxoglutarate carrier: sulfhydryl reagents bind to cysteine-184, and this interaction is enhanced by substrate binding.
AuthorsCapobianco L, Bisaccia F, Mazzeo M, Palmieri F
JournalBiochemistry
PubMed ID8688434
'The interaction of sulfhydryl reagents with the oxoglutarate carrier (OGC) of bovine heart mitochondria was investigated in proteoliposomes reconstituted from purified carrier and lipids. Incubation of the proteoliposomes with maleimides or mercurials led to inhibition of the oxoglutarate carrier protein. The inhibition of oxoglutarate transport by mercurials was removed by ... More
Proximity of sulfhydryl groups in lens proteins. Excimer fluorescence of pyrene-labeled crystallins.
AuthorsSen AC, Chakrabarti B
JournalJ Biol Chem
PubMed ID2387849
'Lens proteins labeled with the -SH-specific reagents N-(1-pyrene)-maleimide (PM) and N-(1-pyrene)-iodo-acetamide (PIA) exhibited pyrene excimer fluorescence around 480 nm. Among the gamma-fractions, only gamma II showed excimer band at room temperature with both probes PM and PIA. As the temperature increased, PM-labeled gamma IIIA, gamma IIIB, and gamma IV also ... More
Topography of the human factor VIII-von Willebrand factor complex.
AuthorsFay PJ, Smudzin TM
JournalJ Biol Chem
PubMed ID2108154
'Factor VIII circulates in noncovalent complex with von Willebrand factor (vWf). The topography of this complex was evaluated by fluorescence energy transfer using factor VIII subunits modified with N-(1-pyrenyl)maleimide (NPM; fluorescence donor) and vWf-derived fragments modified with 7-diethylamino-3-[4''-maleimidylphenyl]-4-methyl coumarin (CPM; fluorescence acceptor). Results from a previous study indicated an interfactor ... More
Initiation of protein synthesis with fluorophore-Met-tRNA(f) and the involvement of IF-2.
AuthorsMcIntosh B, Ramachandiran V, Kramer G, Hardesty B
JournalBiochimie
PubMed ID10727773
'The complicity of initiation factor 2 (IF-2) in causing the observed low incorporation of N-terminal fluorophore from fluorophore-methionyl-tRNA(f) during protein synthesis in an in vitro coupled transcription/translation system was investigated. The low incorporation in comparison to formyl-methionine was not due to the lack of interaction of fluorophore-Met-tRNA(f) with IF-2. Fluorescence ... More
Ceruloplasmin has a distinct active site for the catalyzing glutathione-dependent reduction of alkyl hydroperoxide.
AuthorsCha MK, Kim IH
JournalBiochemistry
PubMed ID10508415
'Ceruloplasmin, a blue multi-copper alpha(2)-glycoprotein found in the plasma of all vertebrates, is capable of oxidizing aromatic amines and ferrous iron. Here, we report that human ceruloplasmin exhibits an alkyl hydroperoxide peroxidase activity, which is independent of the oxidase activity. The site-specific modification of the sulfhydryl of cysteine at position ... More
Pyrene excimer fluorescence in rabbit skeletal alphaalphatropomyosin labeled with N-(1-pyrene)maleimide. A probe of sulfhydryl proximity and local chain separation.
AuthorsBetcher-Lange SL, Lehrer SS
JournalJ Biol Chem
PubMed ID565773
'Rabbit skeletal alphaalphatropomyosin was specificially labeled at cysteine 190 with the fluorescent reagent, N-(1-pyrene)maleimide. Spectroscopically different products were obtained by labeling at pH 6.0 (PyrI-alphaalphaTm) or pH 7.5 (PyrII-alphaalphaTm). PyrII-alphaalphaTm results from a secondary reaction between the N-(1-pyrene)succinimido moiety at cysteine 190 of PyrI-alphaalphaTm and a lysine group on the ... More
Resonance energy transfer: methods and applications.
AuthorsWu P, Brand L
JournalAnal Biochem
PubMed ID8053542
'Resonance energy transfer is widely used in studies of biomolecular structure and dynamics. It provides information about distances on the order of 10 to 100 A and is thus suitable for investigating spatial relationships of interest in biochemistry. The information available from energy transfer studies has been enhanced by the ... More
Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase.
AuthorsYao Y, Yin D, Jas GS, Kuczer K, Williams TD, Schöneich C, Squier TC
JournalBiochemistry
PubMed ID8611584
'In order to investigate the possibility that calmodulin (CaM) may be a principal target of reactive oxygen species (ROS) produced under conditions of oxidative stress, we have examined wheat germ CaM for the presence of highly reactive sites that correlate with the loss of function. Using reversed-phase HPLC and FAB ... More
Changes in the molecular structure of mouse fetal astrocyte nucleosomes produced in vitro by methylmercuric chloride.
AuthorsChoi BH, Simpkins H
JournalEnviron Res
PubMed ID3956461
'The fluorescent probe N-(3-pyrene)maleimide, which specifically labels the cysteine residues of histone H3 within the nucleosome, was used to monitor changes in the nucleosomal structure of mouse fetal astrocytes exposed to varying concentrations of methylmercuric chloride. Methylmercuric chloride treatment (10 microM) for 6 hr produced a significant decrease in the ... More
Refolding of target proteins from a "rigid" mutant chaperonin demonstrates a minimal mechanism of chaperonin binding and release.
AuthorsMizobata T, Kawagoe M, Hongo K, Nagai J, Kawata Y
JournalJ Biol Chem
PubMed ID10837467
'One of the most interesting facets of GroEL-facilitated protein folding lies in the fact that the requirement for a successful folding reaction of a given protein target depends upon the refolding conditions used. In this report, we utilize a mutant of GroEL (GroEL T89W) whose domain movements have been drastically ... More
Topography of nicotinic acetylcholine receptor membrane-embedded domains.
AuthorsBarrantes FJ, Antollini SS, Blanton MP, Prieto M
JournalJ Biol Chem
PubMed ID10967108
'The topography of nicotinic acetylcholine receptor (AChR) membrane-embedded domains and the relative affinity of lipids for these protein regions were studied using fluorescence methods. Intact Torpedo californica AChR protein and transmembrane peptides were derivatized with N-(1-pyrenyl)maleimide (PM), purified, and reconstituted into asolectin liposomes. Fluorescence mapped to proteolytic fragments consistent with ... More
Identification of an essential sulfhydryl group in the ouabain binding site of (Na,K)-ATPase.
AuthorsKirley TL, Lane LK, Wallick ET
JournalJ Biol Chem
PubMed ID3007461
'Ellman''s reagent 5,5''-dithiobis-(2-nitrobenzoic acid) inhibits sodium- and potassium-stimulated ATPase, p-nitrophenyl phosphatase activity, and [3H]ouabain binding to lamb kidney (Na,K)-ATPase. The inactivation of [3H]ouabain binding follows pseudo-first order reaction kinetics at pH values less than or equal to 8.2. The inactivation of [3H]ouabain binding, but not of enzymatic activity, can be ... More
The interaction of platinum complexes with nucleosomes investigated with fluorescent probes.
AuthorsThompson LM, Arquilla M, Simpkins H
JournalBiochim Biophys Acta
PubMed ID6889888
'The fluorescent probes, N,-(3-pyrene)maleimide, which is specific for histone H3, and terbium (Tb3+), which is specific for guanine single-stranded residues in DNA, are used to investigate the interaction of platinum complexes (cis- and trans-dichlorodiammineplatinum(II)) with rat liver and calf thymus nucleosomes. At low concentrations of the drug, lower than most ... More
Detection of the conformational change in the catalytic site of adenosine triphosphatase from beef liver mitochondria by affinity labeling with the dialdehyde derivative of ethenoadenosine triphosphate.
AuthorsWakagi T, Ohta T
JournalJ Biochem (Tokyo)
PubMed ID6218159
'Beef liver mitochondrial F1ATPase was inactivated by the 2'',3''-dialdehyde derivative of ethenoATP (epsilon ATP) in a pseudo-first order reaction. The kinetics of protection of the enzyme against inactivation by various nucleoside triphosphates (NTPs) revealed that the dial-epsilon ATP was bound to the catalytic site as an affinity label. Certain anions ... More
Comparison of the fluorescence and conformational properties of smooth and striated tropomyosin.
AuthorsLehrer SS, Betteridge DR, Graceffa P, Wong S, Seidel JC
JournalBiochemistry
PubMed ID6722112
'In contrast to previous conformational studies with rabbit skeletal and cardiac tropomyosins, (i) when the cysteine side chains of chicken gizzard tropomyosin were reacted with 5,5''-dithiobis(2-nitrobenzoate), an interchain disulfide cross-link was not produced, (ii) when they were labeled with pyrenylmaleimide , excimer fluorescence was not observed, and (iii) when they ... More
Vacuolar accumulation and extracellular extrusion of electrophilic compounds by wild-type and glutathione-deficient mutants of the methylotrophic yeast Hansenula polymorpha.
AuthorsUbiyvovk VM, Maszewski J, Bartosz G, Sibirny AA
JournalCell Biol Int
PubMed ID12972285
'The methylotrophic yeast Hansenula polymorpha CBS4732 leu2 detoxifies electrophilic xenobiotics by glutathione (GSH)-dependent accumulation in vacuoles, as shown by fluorescence microscopy. GSH-dependent and GSH-independent export of xenobiotic derivatives were also demonstrated by high-performance liquid chromatography (HPLC). Conjugates of GSH and N-acetylcysteine with monobromobimane and N-[1-pyrene]maleimide were observed among the HPLC ... More
ADP binding induces long-distance structural changes in the beta polypeptide of the chloroplast ATP synthase.
AuthorsMills DA, Seibold SA, Squier TC, Richter ML
JournalBiochemistry
PubMed ID7742314
'Binding of ADP to the beta polypeptide isolated from the catalytic F1 portion (CF1) of the chloroplast ATP synthase caused an increase of 10-20% in the steady state fluorescence intensity of fluorescent maleimides attached to the cysteine residue at position 63. Fluorescence lifetime distributions indicated that the beta polypeptide switched ... More
Derivatization of thiol-containing compounds.
AuthorsShimada K, Mitamura K
JournalJ Chromatogr B Biomed Appl
PubMed ID7820279
'The determination of thiol-containing compounds in biological fluids is important in biochemistry and clinical chemistry. In this paper, derivatization reagents for thiols are reviewed with respect to their reactivity, selectivity, spectroscopic characteristics and their applicability especially to high-performance liquid chromatography. Derivatization used in ultraviolet and electrochemical detection. The derivatization reagents ... More
Resonance energy transfer between tryptophan 57 in the epsilon subunit and pyrene maleimide labeled gamma subunit of the chloroplast ATP synthase.
AuthorsJohnson EA, Evron Y, McCarty RE
JournalBiochemistry
PubMed ID11327843
'The intrinsic fluorescence of the catalytic portion of the chloroplast ATP synthase (CF1) is quenched when cysteine 322, the penultimate amino acid of the gamma subunit, is specifically labeled with pyrene maleimide (PM). The epsilon subunit of CF1 contains the only two residues of tryptophan, which dominate the intrinsic fluorescence ... More
Transport properties of the multidrug resistance-associated protein (MRP) in human tumour cells.
AuthorsHolló Z, Homolya L, Hegedüs T, Sarkadi B
JournalFEBS Lett
PubMed ID8612802
'In this paper we demonstrate that the expression of the multidrug resistance-associated protein (MRP) in a variety of intact human tumour cells results in the ATP-dependent, mutually exclusive extrusion of both the acetoxymethyl ester and the free anion forms of the fluorescent dye calcein, as well as that of a ... More
Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2.
AuthorsBaez M, Rodríguez PH, Babul J, Guixé V
JournalBiochem J
PubMed ID12927023
'Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with pyrene maleimide (PM) results in a rapid inactivation of the enzyme. The loss of enzyme activity correlates with the incorporation of 2 mol of PM/mol of subunit and the concomitant dissociation of the dimeric enzyme. The two modified residues were identified as Cys-238 ... More
Nanosecond fluorometric investigation of hydrodynamic properties of adenosine triphosphatase from thermophilic bacterium PS3.
AuthorsKinosita K, Ikegami A, Yoshida M, Kagawa Y
JournalJ Biochem (Tokyo)
PubMed ID6219102
'The soluble portion (TF1) of proton-translocating ATPase from thermophilic bacterium PS3 was labeled with a fluorescent dye N-(1-pyrene)maleimide. The decay of fluorescence anisotropy of the adduct showed that TF1 in aqueous solution was characterized by a volume of equivalent sphere of 1,120 nm3. This value is 2.4 times the volume ... More
Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: monomers are inactive but preserve ligand binding properties.
AuthorsGuixé V
JournalArch Biochem Biophys
PubMed ID10775417
'Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with N-(1-pyrenil)maleimide results in an enzyme form that is inactive. However, the rate of modification is drastically reduced in the presence of the allosteric effector MgATP. The stoichiometry of the label incorporation was found to be 2.03 +/- 0.035 mol of the reagent/mol of ... More
Conformational changes within the cytosolic portion of phospholamban upon release of Ca-ATPase inhibition.
AuthorsLi J, Bigelow DJ, Squier TC
JournalBiochemistry
PubMed ID15049694
'Phospholamban (PLB) is a major target of the beta-adrenergic cascade in the heart, functioning to modulate contractile force by altering the rate of calcium re-sequestration by the Ca-ATPase. Functionally, inhibition by PLB binding is manifested by shifts in the calcium dependence of Ca-ATPase activation toward higher calcium levels; phosphorylation of ... More
Functional role of the cysteine 451 thiol group in the M4 helix of the gamma subunit of Torpedo californica acetylcholine receptor.
AuthorsLi L, Schuchard M, Palma A, Pradier L, McNamee MG
JournalBiochemistry
PubMed ID1696834
'Previous chemical modification studies of the acetylcholine receptor [Yee, A.S., Corey, D.E., & McNamee, M.G. (1986) Biochemistry 25, 2110-2119] were extended by using fluorescent N-pyrenylmaleimide to alkylate purified Torpedo californica nicotinic acetylcholine receptor (AChR). Peptide sequencing of the tryptic fragments of the labeled AChR gamma subunit identified cysteines 416, 420, ... More
Structural studies on bacterial luciferase using energy transfer and emission anisotropy.
AuthorsTu SC, Wu CW, Hastings JW
JournalBiochemistry
PubMed ID305259
'The distance between specific sites on bacterial luciferase was estimated by energy transfer. Luciferase was fluorescently labeled by reaction of an essential sulfhydryl group with N-(1-pyrene)maleimide and N-[p-(2-benzoxazolyl)phenyl]meleimide. Both of the modified enzymes bind 8-anilino-1-naphthalenesulfonate (Ans) with affinities similar to that exhibited by the native luciferase. Using each of the ... More
The reaction of N-(1-pyrene)maleimide with sarcoplasmic reticulum.
AuthorsPapp S, Kracke G, Joshi N, Martonosi A
JournalBiophys J
PubMed ID2937461
'The excimer fluorescence of the adduct of N-(1-pyrene)maleimide (PMI) with the Ca2+-ATPase was proposed as a probe of ATPase-ATPase interactions in sarcoplasmic reticulum (Lüdi and Hasselbach, Eur. J. Biochem., 1983, 130:5-8). We tested this proposition by analyzing the spectral properties and stoichiometry of the adducts of pyrenemaleimide with sarcoplasmic reticulum ... More
Fluorescence polarization study of the alpha-ketoglutarate dehydrogenase complex from Escherichia coli.
AuthorsWaskiewicz DE, Hammes GG
JournalBiochemistry
PubMed ID6758846
'The lipoic acids of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli have been modified with two fluorescent probes, N-(1-pyrenyl)-maleimide and 5-[[[(iodoacetyl)amino]ethyl]amino]-naphthylene-1-sulfonic acid. Time-resolved fluorescence polarization of partially labeled complexes (18-77% inhibition of enzyme activity) reveals a complex depolarization process: one component of the anisotropy is characterized by a rotational ... More
Substrate binding stabilizes S-adenosylhomocysteine hydrolase in a closed conformation.
AuthorsYin D, Yang X, Hu Y, Kuczera K, Schowen RL, Borchardt RT, Squier TC
JournalBiochemistry
PubMed ID10933798
'Comparison of crystal structures of S-adenosylhomocysteine (AdoHcy) hydrolase in the substrate-free, NAD(+) form [Hu, Y., Komoto, J., Huang, Y., Gomi, T., Ogawa, H., Takata, Y., Fujioka, M., and Takusagawa, F. (1999) Biochemistry 38, 8323-8333] and a substrate-bound, NADH form [Turner, M. A., Yuan, C.-S., Borchardt, R. T., Hershfield, M. S., ... More
Insight into the conformation of protein folding intermediate(s) trapped by GroEL.
AuthorsTorella C, Mattingly JR, Artigues A, Iriarte A, Martinez-Carrion M
JournalJ Biol Chem
PubMed ID9461576
'Many aspects of the mechanism by which the GroEL/ES chaperonins mediate protein folding are still unclear, including the amount of structure present in the substrate bound to GroEL. To address this issue we have analyzed the susceptibility to limited proteolysis and to alkylation of cysteine residues of mitochondrial aspartate aminotransferase ... More
A study on peroxidative damage of the porcine intestinal brush-border membranes using a fluorogenic thiol reagent, N-(1-pyrene)maleimide.
AuthorsOhyashiki T, Sakata N, Kamata K, Matsui K
JournalBiochim Biophys Acta
PubMed ID1878370
'To examine the effects of lipid peroxidation on the protein conformation in the porcine intestinal brush-border membranes, a fluorogenic thiol reagent, N-(1-pyrene)maleimide (NPM) was employed. By treatment of NPM-labeled membranes with 100 microM ascorbic acid/10 microM Fe2+ in the presence of various concentrations of tert-butyl hydroperoxide (t-BuOOH), the fluorescence intensity ... More
Excimer fluorescence of pyrene-maleimide-labeled tubulin.
AuthorsPanda D, Bhattacharyya B
JournalEur J Biochem
PubMed ID1541290
'Excimer-forming cysteines in tubulin are detected by the presence of excimer fluorescence in N-(1-pyrenyl)maleimide-labeled tubulin. The ratio of excimer/monomer fluorescence of labeled protein remained unchanged upon its dilution. These results indicating that both partner of each pair(s) of cysteine are located in the same subunit. The excimer fluorescence is insensitive ... More
Evidence for the proximity of a cysteine and a lysine residue in the active site of 6-phosphogluconate dehydrogenase from Candida utilis.
AuthorsDallocchio F, Matteuzzi M, Bellini T
JournalItal J Biochem
PubMed ID6414987
'The environment of a cysteine residue in the active site of 6-phosphogluconate dehydrogenase from Candida utilis was investigated by means of N-(3-pyrene) maleimide. The reaction between enzyme and inhibitor results in the modification of one cysteine residue per enzyme subunit, and in the complete inactivation of the enzyme. In a ... More
Chemical modification of lactose repressor protein using N-substituted maleimides.
AuthorsBrown RD, Matthews KS
JournalJ Biol Chem
PubMed ID376506
'Lactose repressor protein has been modified with N-ethylmaleimide, two N-maleimide spin labels, and an N-maleimide fluorophore. The reaction with repressor cysteine residues has been characterized. Approximately 2 of the 3 eq of cysteine/repressor monomer are reactive toward these reagents. Repressor cysteines are reactive toward these reagents in the order cysteine ... More
Analysis of glutathione, glutathione disulfide, cysteine, homocysteine, and other biological thiols by high-performance liquid chromatography following derivatization by n-(1-pyrenyl)maleimide.
AuthorsWinters RA, Zukowski J, Ercal N, Matthews RH, Spitz DR
JournalAnal Biochem
PubMed ID7668373
'The compound N-(1-pyrenyl)maleimide (NPM) reacts with free sulfhydryl groups to form fluorescent derivatives. A new method for measurement of glutathione and other biological thiols utilizing reverse-phase high-performance liquid chromatography to separate and quantify these derivatives is described. Separation and quantification of glutathione, cysteine, homocysteine, cysteinylglycine, and gamma-glutamylcysteine derivatives are achieved. ... More
Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanisms.
AuthorsBottomley SP, Hopkins PC, Whisstock JC
JournalBiochem Biophys Res Commun
PubMed ID9790897
'A number of disease states are attributable to alpha1-antitrypsin polymerisation within the endoplasmic reticulum of hepatocytes and subsequent plasma deficiency. Two distinct mechanisms describing the process of alpha1-antitrypsin polymerisation have been proposed, the loop A-sheet and C-sheet mechanisms. We report fluorescence studies using alpha1-antitrypsin covalently modified with pyrene maleimide. These ... More
Excimer formation of ATPase from sarcoplasmic reticulum labeled with N-(3-pyrene)maleinimide.
AuthorsLüdi H, Hasselbach W
JournalEur J Biochem
PubMed ID6218989
'Sarcoplasmic reticulum ATPase from fast skeletal muscle was labeled in native vesicles with N-(3-pyrene)maleinimide. At labeling ratios larger than 1 mol pyrenemaleinimide/2.5 mol ATPase significant amounts of excimers are detected. Excimer concentration decreases at low, non-solubilizing amounts of detergents (0.2 mg X mg protein-1) and completely disappears after solubilization of ... More
Fluorescence study of N-(3-pyrene)maleimide conjugated to rabbit skeletal F-actin and plasmodium actin polymers.
AuthorsKawasaki Y, Mihashi K, Tanaka H, Ohnuma H
JournalBiochim Biophys Acta
PubMed ID974110
'A fluorescent probe N-(3-pyrene)maleimide was conjugated to rabbit skeletal F-actin at the site of most reactive sulfhydryl group (Cys-373). Its fluorescence anisotropy decay showed a single correlation time of 560 ns at 25 degrees C, which is in a very good agreement with the correlation time of the dansyl-L-cysteine group ... More
Studies on calcium ion-induced conformation changes in the actin-tropomyosin-troponin system by fluorimetry. III. Changes in the conformation of tropomyosin associated with functional states.
AuthorsOhyashiki T, Kanaoka Y, Sekine T
JournalBiochim Biophys Acta
PubMed ID1247580
'The local conformational changes in the tropomyosin molecule under various conditions were studied by means of fluorimetry using SH-directed fluorescent dyes, N-(1-anilinonaphthyl-4)maleimide (ANM) and N-(3-pyrene)maleimide (PRM). 1. The fluorescence intensity, polarization and the emmission maximum of ANM-tropomyosin were found to be susceptible to ionic strength, but in different ways. The ... More
Fluorescence studies on N-(3-pyrene)maleinimide-labeled sarcoplasmic reticulum ATPase in native and solubilized membranes.
AuthorsLüdi H, Hasselbach W
JournalZ Naturforsch [C]
PubMed ID6222551
'Fluorescence polarization and formation of excimers were studied in N-(3-pyrene)maleinimide-labeled sarcoplasmic reticulum vesicles. 1. The polarization of pyrenemaleinimide labeled vesicles does not change with temperature and shows a pronounced decrease at labeling concentrations larger than 1 mol pyrenemaleinimide per 10 mol ATPase. 2. Solubilization of the membrane with myristoylglycerophosphocholine renders ... More
N-termini of EcoRI restriction endonuclease dimer are in close proximity on the protein surface.
'The N-terminal region of EcoRI endonuclease is essential for cleavage yet is invisible in the 2.5 A crystal structure of endonuclease-DNA complex [Kim, Y., Grable, J. C., Love, R., Greene, P. J., Rosenberg, J. M. (1990) Science 249, 1307-1309]. We used site-directed fluorescence spectroscopy and chemical cross-linking to locate the ... More
Segmental flexibility of receptor-bound immunoglobulin E.
AuthorsSlattery J, Holowka D, Baird B
JournalBiochemistry
PubMed ID2936392
'The segmental flexibility of mouse immunoglobulin E (IgE) bound to its high-affinity receptor on membrane vesicles from rat basophilic leukemia cells was compared to that of IgE in solution by measuring the steady-state anisotropy as a function of temperature and viscosity. A monoclonal IgE was used to bind the fluorescent ... More
Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. II. The Gp44/62 clamp loader interacts with a single defined face of the sliding clamp ring.
AuthorsLatham GJ, Bacheller DJ, Pietroni P, von Hippel PH
JournalJ Biol Chem
PubMed ID9395509
'The phage T4 gp45 sliding clamp is a ring-shaped replication accessory protein that is mounted onto DNA in an ATP-dependent manner by the gp44/62 clamp loader. In the preceding paper (Pietroni, P., Young, M. C., Latham, G. J., and von Hippel, P. H. (1997) J. Biol. Chem. 272, 31666-31676), two ... More
Binding of the activating ion Co(II) to myo-inositol monophosphatase monitored by fluorescence and phosphorescence spectroscopy.
AuthorsKwon OS, Churchich JE
JournalJ Protein Chem
PubMed ID9055202
'Two extrinsic probes, pyrene-maleimide and eosin-maleimide, were used to label specific SH groups of the enzyme myo-inositol monophosphatase. The fluorescence of pyrene-monophosphatase is enhanced upon addition of the activating metal ions Co(II) and Mg(II). Co(II) ions bind with a dissociation constant of 4 microM, whereas the apparent activation constant Ka ... More
Excimer formation in pyrenemaleimide-labeled sarcoplasmic reticulum ATPase.
AuthorsLüdi H, Hasselbach W
JournalBiophys J
PubMed ID2952178
Fluorescence energy transfer measurements in the pyruvate dehydrogenase multienzyme complex from Escherichia coli with chemically modified lipoic acid.
AuthorsShepherd GB, Hammes GG
JournalBiochemistry
PubMed ID336083
Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide.
AuthorsJanmey PA
JournalMethods Enzymol
PubMed ID2034138
Role of histone pairs H2A,H2B and H3,H4 in the self-assembly of nucleosome core particles.
AuthorsDaban JR, Cantor CR
JournalJ Mol Biol
PubMed ID7120393
Structural and kinetic study of the self-assembly of nucleosome core particles.
AuthorsDaban JR, Cantor CR
JournalJ Mol Biol
PubMed ID7120392
Structural alterations in the 30 S ribosomal subunit of Escherichia coli observed with the fluorescent probe N-(3-pyrene) maleimide.
AuthorsSchechter N, Elson D, Spitnik-Elson P
JournalFEBS Lett
PubMed ID1100432
N-(3-Pyrene)maleimide: a fluorescent probe of acetylcholine receptor-Triton X-100 aggregates.
AuthorsSator V, Raftery MA, Martinez-Carrion M
JournalArch Biochem Biophys
PubMed ID708079
N-(3-pyrene)maleimide: a long lifetime fluorescent sulfhydryl reagent.