Spectral diffusion experiment with a denatured protein

被引：7

作者：

Ponkratov, VV

Friedrich, J ^{[1
]}

Markovic, D

Scheer, H

Vanderkooi, JM

机构：

[1] Tech Univ Munich, Dept Phys, D-85350 Freising Weihenstephan, Germany

[2] Tech Univ Munich, Lehrstuhl Phys Weihenstephan, D-85350 Freising Weihenstephan, Germany

[3] Dept Biol 1 Bereich Bot, D-80638 Munich, Germany

[4] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2004年 / 108卷 / 03期

关键词：

D O I：

10.1021/jp0359135

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Spectral diffusion broadening of cytochrome c carrying the free-base analogue of heme is investigated in its unfolded state and compared with the corresponding broadening in the native state. Spectral diffusion is much larger in the unfolded state, in comparison to the native state. Interestingly, the time law that governs spectral diffusion changes as the aging time increases, from a power-law behavior in the native state to an apparent logarithmic behavior in the unfolded state.

引用

页码：1109 / 1114

页数：6

共 34 条

[1]

[Anonymous], 1998, ANGEW CHEM, V110, P908

[2]

Bai YW, 2000, PROTEIN SCI, V9, P194

[3] BIPHASIC TRANSITION CURVE ON DENATURATION OF CHICKEN CYSTATIN BY GUANIDINIUM CHLORIDE - EVIDENCE FOR AN INDEPENDENTLY UNFOLDING STRUCTURAL REGION [J].