NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins

Levani Zandarashvili, Alexandre Esadze, Junji Iwahara

Research output: Chapter in Book/Report/Conference proceedingChapter

21 Scopus citations

Abstract

Hydrogen bonds and ion pairs involving side chains play vital roles in protein functions such as molecular recognition and catalysis. Despite the wealth of structural information about hydrogen bonds and ion pairs at functionally crucial sites on proteins, the dynamics of these fundamental chemical interactions are not well understood largely due to the lack of suitable experimental tools in the past. NMR spectroscopy is a powerful tool for investigations of protein dynamics, but the vast majority of NMR methods had been applicable only to the backbone or methyl groups. Recently, a substantial progress has been made in the research on the dynamics of hydrogen bonds and ion pairs involving lysine side-chain NH3 + groups. Together with computational/theoretical approaches, the new NMR methods provide unique insights into the dynamics of hydrogen bonds and ion pairs involving lysine side chains. Here, the methodology and its applications are reviewed.

Original languageEnglish (US)
Title of host publicationBiomolecular Spectroscopy
Subtitle of host publicationAdvances from Integrating Experiments and Theory
PublisherAcademic Press Inc.
Pages37-80
Number of pages44
ISBN (Print)9780124165960
DOIs
StatePublished - 2013

Publication series

NameAdvances in Protein Chemistry and Structural Biology
Volume93
ISSN (Print)1876-1623

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Keywords

  • Computation
  • Hydrogen bonds
  • Internal motions
  • Ion pairs
  • J coupling
  • Lysine
  • Molecular dynamics
  • Side-chain dynamics

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

Zandarashvili, L., Esadze, A., & Iwahara, J. (2013). NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins. In Biomolecular Spectroscopy: Advances from Integrating Experiments and Theory (pp. 37-80). (Advances in Protein Chemistry and Structural Biology; Vol. 93). Academic Press Inc.. https://doi.org/10.1016/B978-0-12-416596-0.00002-6