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

  1. Author:
    Cierpicki, T.
    Zhukov, I.
    Byrd, R. A.
    Otlewski, J.

  2. Author Address

    Univ Wroclaw, Inst Biochem & Mol Biol, Lab Prot Engn, Tamka 2, PL-50137 Wroclaw, Poland Univ Wroclaw, Inst Biochem & Mol Biol, Lab Prot Engn, PL-50137 Wroclaw, Poland Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland NCI, Struct Biophys Lab, Frederick, MD 21702 USA Cierpicki T Univ Wroclaw, Inst Biochem & Mol Biol, Lab Prot Engn, Tamka 2, PL-50137 Wroclaw, Poland
    1. Year: 2002
  2. Journal: Journal of Magnetic Resonance
    1. 157
    2. 2
    3. Pages: 178-180
  4. Type of Article: Article
  1. Abstract:

    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).

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