Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy-Reference-Cited by-同舟云学术

Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy

Published:2009-11-02 Issue:2 Volume:147 Page:191-200
ISSN:0021-924X
Container-title:Journal of Biochemistry
language:en
Short-container-title:Journal of Biochemistry

Author:

Otosu T.,Nishimoto E.,Yamashita S.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://academic.oup.com/jb/article-pdf/147/2/191/2326974/mvp175.pdf

Reference33 articles.

1. The extraordinary ligand binding properties of human serum albumin

2. Binding of the General Anesthetics Propofol and Halothane to Human Serum Albumin

3. Ultrafast Solvation Dynamics of Human Serum Albumin: Correlations with Conformational Transitions and Site-Selected Recognition

4. Anion-induced refolding of human serum albumin under low pH conditions

5. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation

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