Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons

被引：77

作者：

Cierpicki, T

Zhukov, I

Byrd, RA

Otlewski, J

机构：

[1] Univ Wroclaw, Inst Biochem & Mol Biol, Lab Prot Engn, PL-50137 Wroclaw, Poland

[2] Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland

[3] NCI, Struct Biophys Lab, Frederick, MD 21702 USA

来源：

JOURNAL OF MAGNETIC RESONANCE | 2002年 / 157卷 / 02期

关键词：

amide proton temperature coefficients; chemical shifts; hydrogen bonds; ubiquitin;

D O I：

10.1006/jmre.2002.2597

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Analysis of amide proton temperature coefficients (Deltasigma(HN)/DeltaT) in human ubiquitin shows their usefulness in indicating hydrogen bonds. The availability of a very accurate solution structure of ubiquitin enables the precise determination of hydrogen bonds and increases the reliability of the analysis of chemical shift temperature gradients. Values of Deltasigma(HN)/DeltaT more positive than -4.6 ppb/K are very good indicators of hydrogen bonds. Additionally, a weak temperature dependence of non-hydrogen-bonded amides was observed for amide protons that are significantly shifted upfield. We observed that temperature gradients of amide protons involved in short hydrogen bonds are related to donor-acceptor distances. (C) 2002 Elsevier Science (USA).

引用

页码：178 / 180

页数：3

共 13 条

[1] Extracting information from the temperature gradients of polypeptide NH chemical shifts .1. The importance of conformational averaging [J].