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 Citations (Scopus)

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 publicationAdvances in Protein Chemistry and Structural Biology
PublisherAcademic Press Inc.
Pages37-80
Number of pages44
Volume93
ISBN (Print)9780124165960
DOIs
StatePublished - 2013

Publication series

NameAdvances in Protein Chemistry and Structural Biology
Volume93
ISSN (Print)18761623

Fingerprint

Pair Bond
Lysine
Protons
Hydrogen bonds
Nuclear magnetic resonance
Ions
Proteins
Molecular recognition
Catalysis
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Research

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology

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 Advances in Protein Chemistry and Structural Biology (Vol. 93, 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

NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins. / Zandarashvili, Levani; Esadze, Alexandre; Iwahara, Junji.

Advances in Protein Chemistry and Structural Biology. Vol. 93 Academic Press Inc., 2013. p. 37-80 (Advances in Protein Chemistry and Structural Biology; Vol. 93).

Research output: Chapter in Book/Report/Conference proceedingChapter

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