PROBING PROTEIN-STRUCTURE AND DYNAMICS BY TRITIUM NMR

被引：1

作者：

OCONNELL, TM ^{[1
]}

WILLIAMS, PG ^{[1
]}

GERIG, JT ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,LAWRENCE BERKELEY LAB 75-123,NATL TRITIUM LABELING FACIL,BERKELEY,CA 94720

来源：

JOURNAL OF LABELLED COMPOUNDS & RADIOPHARMACEUTICALS | 1993年 / 33卷 / 05期

关键词：

TRITIUM NMR; TOSYLCHYMOTRYPSIN; NMR REPORTER GROUPS; PROTEIN;

D O I：

10.1002/jlcr.2580330503

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Tritium nmr spectroscopy of specifically tritiated tosylchymotrypsin has been used to examine the properties of the tosyl group in this protein. The unavoidable presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of relaxation behavior of tritiated species present were used in conjunction with models developed from crystallographic results to interpret the observations made. These analyses suggest that the tosyl group of tosylchymotrypsin at pH 4 is highly mobile in solution and occupies the location in the protein that is observed in the crystalline state only about 50% of the time.

引用

页码：371 / 380

页数：10

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