MULTIDIMENSIONAL NUCLEAR-MAGNETIC-RESONANCE METHODS TO PROBE METAL ENVIRONMENTS IN PROTEINS

被引：5

作者：

CANTERS, GW ^{[1
]}

HILBERS, CW ^{[1
]}

VANDEKAMP, M ^{[1
]}

WIJMENGA, SS ^{[1
]}

机构：

[1] UNIV NIJMEGEN, NIJMEGEN SON RES CTR, BIOPHYS CHEM LAB, 6525 ED NIJMEGEN, NETHERLANDS

来源：

METALLOBIOCHEMISTRY, PT D: PHYSICAL AND SPECTROSCOPIC METHODS FOR PROBING METAL ION ENVIRONMENTS IN METALLOPROTEINS | 1993年 / 227卷

关键词：

D O I：

10.1016/0076-6879(93)27011-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

This chapter discusses methods to obtain information about metal sites in proteins by means of nuclear magnetic resonance (NMR) techniques. NMR spectroscopy has developed into a powerful method to study structures both of metal environments in proteins and of proteins in general. The application of NMR in chemistry and biochemistry is discussed in the chapter. An introduction to general NMR methodology used for protein structure determination is also presented. The chapter also discusses the structure of metal environments in proteins. The use of pH variations to identify metal ligands, techniques to probe the environment of a metal inside a protein for paramagnetic and diamagnetic metal ions, and extrinsic ligands are described. It discusses time-dependent phenomena—namely, conformational equilibria, NH exchange rates, and NMR relaxation times. It also focuses on probing the oxidation state of a metal site and changes thereof. Finally, modeling metal sites in proteins is also presented in the chapter. © 1993, Elsevier Inc. All rights reserved.

引用

页码：244 / 290

页数：47

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