NMR structural studies of glutathione S-transferase

被引：22

作者：

Lian, LY ^{[1
]}

机构：

[1] Univ Leicester, Biol NMR Ctr, Leicester LE1 9HN, Leics, England

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 1998年 / 54卷 / 04期

关键词：

glutathione S-transferase; NMR; high resolution phenylalanines; isotopic labelling; conformational changes; dynamics;

D O I：

10.1007/s000180050164

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 use of nuclear magnetic resonance (NMR) spectroscopy for the structure determination of small proteins is now widely recognized; what is less frequently reported is the application of NMR techniques for high-resolution studies of large proteins (M-r larger than 30 kD). We demonstrate here how an integrated approach, using heteronuclear NMR and X-ray crystallography, can provide useful and biologically important information for large protein systems. The dynamic features of the human Al-1 glutathione S-tranferase and the role of the C-terminal region are being probed by NMR; in the X-ray crystal structure, the electron densities for this region of the protein are uninterpretable.

引用

页码：359 / 362

页数：4

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