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Volumn 19, Issue 6, 2000, Pages 431-439

Native fluorescence and Mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride

(5) Viallet, Pierre M a,b Vo Dinh, Tuan b Ribou, Anne Cécile a Vigo, Jean a Salmon, Jean Marie a

a UNIVERSITÉ DE PERPIGNAN (France)

b OAK RIDGE NATIONAL LABORATORY (United States)

Author keywords

Conformational changes; Energy transfer; Fluorescence quenching; Fluorescence spectra; Protein folding; Structural biology; Tryptophan

Indexed keywords

BOVINE SERUM ALBUMIN; GUANIDINE; HUMAN SERUM ALBUMIN; TRYPTOPHAN;

ARTICLE; CATTLE; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PH; PROTEIN FOLDING; PROTEIN STRUCTURE;

ANIMALS; CALCIUM; CATTLE; FLUORESCENT DYES; GUANIDINE; HUMANS; INDOLES; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

BOS TAURUS; BOVINAE;

EID: 0034518920 PISSN: 02778033 EISSN: None Source Type: Journal
DOI: 10.1023/A:1026589012724 Document Type: Article

Times cited : (35)

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