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The effect of the cosolvent trifluoroethanol on a tryptophan side chain orientation in the hydrophobic core of troponin CPurified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activityFemtosecond dynamics of rubredoxin: tryptophan solvation and resonance energy transfer in the protein.Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Fast-gated intensified charge-coupled device camera to record time-resolved fluorescence spectra of tryptophan.Ultrafast fluorescence spectroscopy via upconversion applications to biophysicsQuasi-static self-quenching of Trp-X and X-Trp dipeptides in water: ultrafast fluorescence decay.Role of the membrane in the formation of heme degradation products in red blood cells.Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.The red-edge effects: 30 years of exploration.Bacteriophage φ6--structure investigated by fluorescence Stokes shift spectroscopyEffects of Visible-Light Irradiation of Protoporphyrin IX on the Self-Assembly of Tubulin HeterodimersFemtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching.Wide-field medium-repetition-rate multiphoton microscopy reduces photodamage of living cells.Label-free imaging of amyloids using their intrinsic linear and nonlinear optical properties.Photophysical processes in single molecule organic fluorescent probes.Experimental and computational characterization of photosensitized conformational effects mediated by protoporphyrin ligands on human serum albumin.Tryptophan properties in fluorescence and functional stability of plasminogen activator inhibitor 1.Interpretation of fluorescence decays using a power-like model.Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm Nereis diversicolor upon Ca2+ or Mg2+ binding.Conformational effects on tryptophan fluorescence in cyclic hexapeptides.Fluorescence lifetime imaging of endogenous fluorophores in histopathology sections reveals differences between normal and tumor epithelium in carcinoma in situ of the breast.Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stabilityExcited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin.Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling.Tryptophan conformations associated with partial unfolding in ribonuclease T1Dynamic functional contribution of the water channel AQP5 to the water permeability of peripheral lens fiber cells.Stereodifferentiation in the intramolecular singlet excited state quenching of hydroxybiphenyl-tryptophan dyads.Electrode reactions in slowly relaxing media.Biointeractions of Herbicide Atrazine with Human Serum Albumin: UV-Vis, Fluorescence and Circular Dichroism Approaches.Structure and dynamics of the gammaM4 transmembrane domain of the acetylcholine receptor in lipid bilayers: insights into receptor assembly and function.
P2860
Q27655623-22D69E57-E8BC-462A-ACA3-A4163D75C43FQ28486409-2A5624C9-8006-425D-A958-C1FA58433B39Q30329283-E0B5B8F1-DF07-4EEF-85E2-905935C5DD93Q30376126-414EA174-79A6-426F-B8D3-ECA29B133686Q31079923-EC93C188-07F0-4FEE-BF8E-F086418DA653Q33400915-5500E8C1-C685-49B9-8891-DF2970099189Q33496900-F3D93A8F-E28B-46ED-A05E-38757210912BQ33641520-3952AA26-258C-4E80-8C18-AB486EE63D2FQ34480953-089A05F8-352F-4258-87B9-FC791C2D95DAQ34509135-841D1D57-540E-43F4-ABCD-D6D20E01A274Q35798723-8427FDCA-A7E9-4EA0-967F-353CA9C155F1Q36094835-BE43D77D-B688-48A9-859D-5D37CF532911Q36226199-EC085E3A-A7C3-4004-B063-9B35BAE1537BQ37057637-471E68C2-CC88-4F4E-A769-EEAD59408A18Q37671903-04ACEF21-EBA2-422F-9554-E0CFD5B68810Q38154104-859C7C28-70F2-4106-A605-7F25861997A3Q38911727-DD605A2B-25EE-4312-AFBE-74E0AC6DBA5DQ40243697-ED63357E-4C1B-4255-B21C-7300888E9926Q40243947-B0F76DCC-B287-4B60-9E89-3F5CFBF3A80EQ40252653-911F8D29-F1B6-414B-A3D9-563E8BBB4089Q40285260-241AB5AC-15A7-4BE0-B197-DA3278A8CDE3Q41553767-07C2B933-0CF5-474A-ABC9-5B02CA2DAC36Q42040491-7925548F-2174-4159-BD8D-D29F1AE351F0Q42159663-5DD0A35C-C4EA-4E80-8454-0DA6FAD67259Q42183666-02F85632-5C18-4883-BC0C-3921317BD4CEQ42563238-155B88DD-08A4-496C-B002-353D9202DCA6Q46265541-D6A59C37-CCAF-4B55-B8BE-7676721BEBACQ46282221-3F726F39-24AE-408D-A747-77B5A299FD63Q47428261-18D8788F-7E56-435A-AB4D-E19DCFF191DAQ48043510-72E368A1-6532-42BF-A348-D420C9306FADQ50724222-12B05B3D-FBE7-493D-A82E-EDBEB264E7E2
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
On spectral relaxation in proteins.
@ast
On spectral relaxation in proteins.
@en
On spectral relaxation in proteins.
@nl
type
label
On spectral relaxation in proteins.
@ast
On spectral relaxation in proteins.
@en
On spectral relaxation in proteins.
@nl
prefLabel
On spectral relaxation in proteins.
@ast
On spectral relaxation in proteins.
@en
On spectral relaxation in proteins.
@nl
P1476
On spectral relaxation in proteins
@en
P2093
J R Lakowicz
P2860
P304
P356
10.1562/0031-8655(2000)072<0421:OSRIP>2.0.CO;2
P577
2000-10-01T00:00:00Z