caa a22 4500 47574389X CHVBK 20180406123507.0 cr unu---uuuuu 170329e20000801xx s 000 0 eng 10.1023/A:1026589012724 doi (NATIONALLICENCE)springer-10.1023/A:1026589012724 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 [Elektronische Daten] [Pierre Viallet, Tuan Vo-Dinh, Anne-Cécile Ribou, Jean Vigo, Jean-Marie Salmon] Changes in the fluorescence spectrum of tryptophans Trp 134 and Trp 212 in bovine serum albumin (BSA) and of Trp 214 of human serum albumin in the presence of the chaotropic agent guanidine hydrochloride (Gnd) were studied. A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. Changes occurring when the Gnd concentration is decreased stepwise cover a larger concentration scale of Gnd than the reverse protocol, allowing one to suggest that the resulting conformational changes in the subdomain IA of BSA involve at least three different steps. Plenum Publishing Corporation, 2000 Fluorescence spectra nationallicence fluorescence quenching nationallicence energy transfer nationallicence protein folding nationallicence conformational changes nationallicence structural biology nationallicence tryptophan nationallicence Viallet Pierre Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut Vo-Dinh Tuan Advanced Monitoring Development Group, Life Sciences Division, Oak Ridge National Laboratory, 37831-6101, Oak Ridge, Tennessee aut Ribou Anne-Cécile Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut Vigo Jean Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut Salmon Jean-Marie Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/6(2000-08-01), 431-439 0277-8033 19:6<431 2000 19 10930 https://doi.org/10.1023/A:1026589012724 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1026589012724 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Viallet Pierre Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut NATIONALLICENCE 700 1- Vo-Dinh Tuan Advanced Monitoring Development Group, Life Sciences Division, Oak Ridge National Laboratory, 37831-6101, Oak Ridge, Tennessee aut NATIONALLICENCE 700 1- Ribou Anne-Cécile Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut NATIONALLICENCE 700 1- Vigo Jean Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut NATIONALLICENCE 700 1- Salmon Jean-Marie Quantitative Microfluorometry Group, Laboratory of Physicochemical Biology of Integrated Systems, University of Perpignan, F-66840, Perpignan, France aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/6(2000-08-01), 431-439 0277-8033 19:6<431 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer