Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure

被引：85

作者：

Mittermaier, A

Kay, LE

Forman-Kay, JD

机构：

[1] Hosp Sick Children, Struct Biol & Biochem Programme, Toronto, ON M5G 1X8, Canada

[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada

[3] Univ Toronto, Protein Engn Network Ctr Excellence, Toronto, ON M5S 1A8, Canada

[4] Univ Toronto, Dept Med Genet, Toronto, ON M5S 1A8, Canada

[5] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada

来源：

JOURNAL OF BIOMOLECULAR NMR | 1999年 / 13卷 / 02期

基金：

加拿大自然科学与工程研究理事会; 英国医学研究理事会;

关键词：

order parameters; packing density; protein dynamics; surface accessibility;

D O I：

10.1023/A:1008387715167

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：

Methyl axis (S-axis(2)) and backbone NH (S-NH(2)) Order parameters derived from eight proteins have been analyzed. Similar distribution profiles for Ala S-axis(2) and S-NH(2) Order parameters were observed. A good correlation between the two S-axis(2), values of Val and Leu methyl groups is noted, although differences between order parameters can arise. The relation of S-axis(2), or S-NH(2) to solvent accessibility and packing density has also been investigated. Correlations are weal;, likely reflecting the importance of collective, non-local motions in proteins. The lack of correlation between these simple structural parameters and dynamics emphasizes the importance of motional studies to fully characterize proteins.

引用

页码：181 / 185

页数：5

共 35 条

[31] Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding [J].