High-resolution nuclear magnetic resonance studies of proteins

被引：69

作者：

Jonas, J ^{[1
]}

机构：

[1] Univ Illinois, Beckman Inst Adv Sci & Technol, Urbana, IL 61801 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1595卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

high resolutio; nuclear magnetic resonance; high pressure; protein; unfolding; folding intermediate;

D O I：

10.1016/S0167-4838(01)00341-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The combination of advanced high-resolution nuclear magnetic resonance (NMR) techniques with high-pressure capability represents a powerful experimental tool in studies of protein folding. This review is organized as follows: after a general introduction of high-pressure, high-resolution NMR spectroscopy of proteins, the experimental part deals with instrumentation. The main section of the review is devoted to NMR studies of reversible pressure unfolding of proteins with special emphasis on pressure-assisted cold denaturation and the detection of folding intermediates. Recent studies investigating local perturbations in proteins and the experiments following the effects of point mutations on pressure stability of proteins are also discussed. Ribonuclease A, lysozyme, ubiquitin, apomyoglobin, alpha-lactalbumin and troponin C were the model proteins investigated. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：145 / 159

页数：15

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