Peptides in BioNMR Research

Authors

  • Oliver Zerbe Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland;, Email: oliver.zerbe@chem.uzh.ch
  • Christian Baumann Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland
  • Matthias Schuster Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland
  • Kerstin Moehle Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland
  • Kathryn K. Oi Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland
  • Erich Michel Department of Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland

DOI:

https://doi.org/10.2533/chimia.2021.505

PMID:

34233813

Keywords:

Antibiotic, Gpcrs, Nmr, Lpt, Repeat protein

Abstract

Heteronuclear NMR in combination with isotope labelling is used to study folding of polypeptides induced by metals in the case of metallothioneins, binding of the peptidic allosteric modulator ?-TIA to the human G-protein coupled ?1b adrenergic receptor, the development of therapeutic drugs that interfere with the biosynthesis of the outer membrane of Gram-negative bacteria, and a system in which protein assembly is induced upon peptide addition. NMR in these cases is used to derive precise structural data and to study the dynamics.

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Published

2021-06-30

How to Cite

[1]
O. Zerbe, C. Baumann, M. Schuster, K. Moehle, K. K. Oi, E. Michel, Chimia 2021, 75, 505, DOI: 10.2533/chimia.2021.505.