THE USE OF FLUORESCENCE METHODS TO MONITOR UNFOLDING TRANSITIONS IN PROTEINS

被引：459
作者：
EFTINK, MR
机构：
[1] Department of Chemistry, University of Mississippi
来源：
BIOPHYSICAL JOURNAL | 1994年 / 66卷 / 02期
基金：
美国国家科学基金会;
关键词：
D O I：
10.1016/S0006-3495(94)80799-4
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
This article discusses several strategies for the use steady-state and time-resolved fluorescence methods to monitor unfolding transitions in proteins. The assumptions and limitations of several methods are discussed. Simulations are presented to show that certain fluorescence observables directly track the population of states in an unfolding transition, whereas other observables skew the transition toward the dominant fluorescing species. Several examples are given, involving the unfolding of Staphylococcal aureus nuclease A, in which thermodynamic information is obtained for the temperature and denaturant induced transitions in this protein.
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收藏
页码：482 / 501
页数：20
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