THE USE OF SELECTIVE DEUTERATION FOR THE SEQUENCE SPECIFIC H-1-NMR ASSIGNMENT OF LARGER PROTEINS

被引：8

作者：

ARROWSMITH, CH

TREATCLEMONS, L

SZILAGYI, L

PACHTER, R

JARDETZKY, O

机构：

[1] Stanford Magnetic Resonance Laboratory, Stanford University, Stanford, California

来源：

MAKROMOLEKULARE CHEMIE-MACROMOLECULAR SYMPOSIA | 1990年 / 34卷

关键词：

D O I：

10.1002/masy.19900340104

中图分类号：

O63 [高分子化学（高聚物）];

学科分类号：

070305 ; 080501 ; 081704 ;

摘要：

The possibility of extending NMR methods for structure determination to larger proteins (MW > 10 kD) depends on the development of isotopic labeling protocols for the simplification of their NMR spectra (isotopic spectral editing). We describe here the successful use of selective deuteration to obtain sequence specific assignments for (thus far) more than 50% of the residues of the trp repressor protein (25 kD). This is the largest protein for which detailed sequence specific assignments have been attempted to‐date. Copyright © 1990 Hüthig & Wepf Verlag

引用

页码：33 / 46

页数：14

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