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Fluorescence lifetime distribution of folded and unfolded proteins

Gratton, E. ; Silva, N. ; Mei, G. ; Rosato, N. ; Savini, I. ; Finazzi-Agro, A.

International journal of quantum chemistry, 1992-06, Vol.42 (5), p.1479-1489 [Periódico revisado por pares]

New York: John Wiley & Sons, Inc

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Título:
Fluorescence lifetime distribution of folded and unfolded proteins
Autor: Gratton, E. ; Silva, N. ; Mei, G. ; Rosato, N. ; Savini, I. ; Finazzi-Agro, A.
Assuntos: Biological and medical sciences ; Chemistry ; Chemistry, Physical ; Fundamental and applied biological sciences. Psychology ; Mathematics ; Mathematics, Interdisciplinary Applications ; Molecular biophysics ; Physical Sciences ; Physics ; Physics, Atomic, Molecular & Chemical ; Quantum Science & Technology ; Science & Technology ; Spectroscopy : techniques and spectras
É parte de: International journal of quantum chemistry, 1992-06, Vol.42 (5), p.1479-1489
Notas: ArticleID:QUA560420522
ark:/67375/WNG-XVLC61CJ-P
istex:CBB024627D60F9BABD586668BD7C0F64DE27F7C9
Descrição: Time‐resolved fluorescence of single tryptophan proteins have demonstrated the complexity of protein dynamic and protein structure. In particular, for some single tryptophan proteins, their fluorescence decay is best described by a distribution of fluorescence lifetimes rather than one or two lifetimes. Such results have provided further confirmation that the protein system is one which fluctuates between a hierarchy of many conformational substates. With this scenario as a theoretical framework, the correlations between protein dynamic and structure are investigated by studying the time‐resolved fluorescence and anisotropy decay of holo and apo human superoxide dismutase (HSOD) at different denaturant concentrations. As a function of guanidine hydrochloride (GdHCl), the width of the fluorescence lifetime distribution of HSOD displays a maximum which is not coincident with the fully denatured form of HSOD at 6.5M GdHCl. Furthermore, the width of the fluorescence lifetime distribution for the fully denatured forms of holo and apo HSOD is greater than that of the native forms.
Editor: New York: John Wiley & Sons, Inc
Idioma: Inglês

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Fluorescence lifetime distribution of folded and unfolded proteins

Gratton, E. ; Silva, N. ; Mei, G. ; Rosato, N. ; Savini, I. ; Finazzi-Agro, A.

New York: John Wiley & Sons, Inc

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