Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

被引：250

作者：

Pollack, L ^{[1
]}

Tate, MW

Darnton, NC

Knight, JB

Gruner, SM

Eaton, WA

Austin, RH

机构：

[1] Cornell Univ, Atom & Solid State Phys Lab, Ithaca, NY 14853 USA

[2] Princeton Univ, Dept Phys, Princeton, NJ 08544 USA

[3] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 18期

关键词：

D O I：

10.1073/pnas.96.18.10115

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.

引用

页码：10115 / 10117

页数：3

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