The fluorescence decay of tryptophan residues in native and denatured proteins.
about
Conformational changes induced in the Tet repressor protein TetR(B) upon operator or anhydrotetracycline binding as revealed by time-resolved fluorescence spectroscopy on single tryptophan mutants.Spectral enhancement of proteins: biological incorporation and fluorescence characterization of 5-hydroxytryptophan in bacteriophage lambda cI repressor.Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein.Tryptophan phosphorescence at room temperature as a tool to study protein structure and dynamics.Distribution of distances between the tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids.Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins.The effect of Glu75 of staphylococcal nuclease on enzyme activity, protein stability and protein unfolding.Flash photolysis of human serum albumin: characterization of the indole triplet absorption spectrum and decay at ambient temperature.On spectral relaxation in proteins.Resolution of fluorescence intensity decays of the two tryptophan residues in glutamine-binding protein from Escherichia coli using single tryptophan mutants.Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutantsProgressive rearrangement of subtilisin Carlsberg into orderly and inflexible conformation with Ca(2+) binding.What causes hyperfluorescence: folding intermediates or conformationally flexible native states?The broken ring: reduced aromaticity in Lys-Trp cations and high pH tautomer correlates with lower quantum yield and shorter lifetimesFrequency domain measurements of the fluorescence lifetime of ribonuclease T1.Picosecond time-resolved fluorescence of ribonuclease T1. A pH and substrate analogue binding study.Fluorescence lifetime studies with staphylococcal nuclease and its site-directed mutant. Test of the hypothesis that proline isomerism is the basis for nonexponential decaysResolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants.Molecular dynamics of tryptophan in ribonuclease-T1. II. Correlations with fluorescence.Conformational heterogeneity of creatine kinase determined from phase resolved fluorometry.Approaches to teaching fluorescence spectroscopy.Molecular dynamics of tryptophan in ribonuclease-T1. I. Simulation strategies and fluorescence anisotropy decay.Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state.Time resolved quenching study of serine-195 labeled alpha-chymotrypsin.Heterogeneity and dynamics of protein conformation revealed by fluorescence decay kinetics of tryptophan residues [proceedings]Structure of a rapidly formed intermediate in ribonuclease T1 folding.Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease a from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry.Binding of a chiral drug to a protein: an investigation of the 2-(3-benzoylphenyl)propionic acid/bovine serum albumin system by circular dichroism and fluorescence.Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.3D structure, dynamics, and activity of synthetic analog of the peptaibiotic trichodecenin I.Fluorescence studies on the coat protein of alfalfa mosaic virus.Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albumin.A steady-state and time-resolved fluorescence, circular dichroism study on the binding of myricetin to bovine serum albumin.Conformational studies of a hyperthermostable enzyme.Origin of tryptophan fluorescence lifetimes. Part 2: fluorescence lifetimes origin of tryptophan in proteins.The binding affinity of amino acid-protein: hydroxyproline binding site I on human serum albumin.Distance-dependent fluorescence quenching of tryptophan by acrylamide.Fluorescence resonance energy transfer between bovine serum albumin and fluoresceinamine.
P2860
Q30327036-F46AC4F7-081D-4461-AAAA-ECE827FA5187Q30336321-18DDF13F-336B-4758-BD33-AE94B1E86CDEQ30365005-56ECE642-2A50-4B7B-84F4-F4270C624A99Q30383066-E644C75F-72A4-46C3-9416-0E0625DC879AQ30444048-64EB7A57-3C9C-4B4E-9B05-8C244F9B5EC2Q30447215-7246D124-43A8-4AEB-BA08-93FF2BA54760Q30674218-AE423FD1-40DA-4D33-A979-FF5A10D6D084Q33966019-A0599300-12FC-4983-8B80-6C855FD16523Q34068451-13999FCC-1821-4F94-B15A-BD75BEAD17AAQ34087914-4A7ED916-D2C8-4EFB-94A6-EF2E2741E21FQ34126299-581D70A8-9913-4B05-BE35-F274262333A3Q34176895-3AAB8389-2CE1-4005-B3D8-9CEBC4FD0CCEQ34178343-A97DA653-351A-4B10-B650-165BAD61C904Q34194365-76176774-79C4-4DC5-ABFD-B055170452B1Q34259425-DED73A7A-F2DE-41EE-A9E5-BD89D956A6A7Q34259457-0E35101D-0966-4C7A-ACCF-A9A3F9379658Q34261382-76FAFDEF-C297-4A69-BA27-FD7BCDC28ECCQ36277734-1589B036-0F46-4D39-9EE7-39478157E2FCQ39618706-6D73A0EE-DFD3-4809-92D9-E5F7AC683071Q39638771-BBDB081E-1C8C-4F5C-9834-8C23E8BFED97Q39654447-67B144CD-606D-461C-9B65-1C7C27F84D93Q41186403-6F2E6825-0524-4EEA-80C1-842506655201Q42184621-32E1B3C5-77C5-4BC3-B301-826CA8A5212AQ42207996-E19E7CBD-A21F-4C7A-992B-012336B8094DQ42421645-5D004907-F73F-413C-A3FA-165A175B73F6Q42842114-97FC07DD-3DDD-45CA-87B4-4C8B8CF99629Q43016354-045BE8E8-CF6E-4F0B-92C0-898BBCC9AB00Q43265758-93276B67-39B9-458F-8128-A284F75B570BQ43877583-50B5D191-0599-4C9F-A5A5-56FE23DF0879Q44972359-5A330182-7AC6-4D20-BE81-8B901B839736Q45832809-F03847E8-045B-4026-AB64-D3E59B09E486Q45904483-12AC46A5-9A87-4D87-942D-E6A25852E5EBQ45990806-11A4CD49-5185-43C2-B304-D6FF957013D9Q46785603-80F7D1AF-7560-4AF1-A5D0-3CB9340D7F76Q47880161-B7810C48-5D7A-42A1-8160-DECAF2CF61F7Q51323550-C8CDA8A1-2C70-4FCB-A322-6C90CD2748C6Q52371821-A29BC977-59D6-4666-A225-194C9AD57D81Q53164052-AF99AAE8-8D75-4FC7-931D-0A3CED0844E3
P2860
The fluorescence decay of tryptophan residues in native and denatured proteins.
description
1976 nî lūn-bûn
@nan
1976 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
name
The fluorescence decay of tryptophan residues in native and denatured proteins.
@ast
The fluorescence decay of tryptophan residues in native and denatured proteins.
@en
type
label
The fluorescence decay of tryptophan residues in native and denatured proteins.
@ast
The fluorescence decay of tryptophan residues in native and denatured proteins.
@en
prefLabel
The fluorescence decay of tryptophan residues in native and denatured proteins.
@ast
The fluorescence decay of tryptophan residues in native and denatured proteins.
@en
P1476
The fluorescence decay of tryptophan residues in native and denatured proteins.
@en
P2093
A Grinvald
I Z Steinberg
P304
P356
10.1016/0005-2795(76)90210-5
P407
P577
1976-04-01T00:00:00Z