MEASUREMENT OF 2-BOND AND 3-BOND C-13-H-1 J-COUPLINGS TO THE C-DELTA CARBONS OF LEUCINE RESIDUES IN STAPHYLOCOCCAL NUCLEASE

被引：43

作者：

VUISTER, GW ^{[1
]}

YAMAZAKI, T ^{[1
]}

TORCHIA, DA ^{[1
]}

BAX, A ^{[1
]}

机构：

[1] NIDR,BONE RES BRANCH,BETHESDA,MD 20892

来源：

JOURNAL OF BIOMOLECULAR NMR | 1993年 / 3卷 / 03期

关键词：

3D NMR; LONG-RANGE J-COUPLING; CARBON CARBON J-COUPLING; CHI-2 TORSION ANGLE; STEREOSPECIFIC ASSIGNMENT; PROTEIN DYNAMICS;

D O I：

10.1007/BF00212516

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：

A new H-1-detected 3D NMR experiment is described that permits quantitative measurement of two- and three-bond C-13-H-1 couplings in proteins with selectively C-enriched methyl sites. The method is demonstrated for staphylococcal nuclease selectively [5,5 C-13]-labeled in all 11 leucine positions and ligated with thymidine 3',5'-biphosphate and Ca2+. Two- and three-bond C-13 methyl-proton couplings are reported and, together with the measured three-bond J(CalphaCdelta) in uniformly C-13-enriched staphylococcal nuclease, the chi2-angles and the stereospecific assignments of the C(delta) methyl group with respect to the prochiral beta-protons were determined. The same residues that were previously found to have high degrees of internal mobility on the basis of C-13 relaxation times have measured coupling constants that are indicative of motional averaging.

引用

页码：297 / 306

页数：10

共 34 条

[11] DETERMINATION OF PROTON-PROTON COUPLING-CONSTANTS IN C-13-LABELED MOLECULES [J].