Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Deborah E. Shalev*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

4 Scopus citations

Abstract

Metal chelation can provide structural stability and form reactive centers in metalloproteins. Approximately one third of known protein structures are metalloproteins, and metal binding, or the lack thereof, is often implicated in disease, making it necessary to be able to study these systems in detail. Peptide-metal complexes are both present in nature and can provide a means to focus on the binding region of a protein and control experimental variables to a high degree. Structural studies of peptide complexes with metal ions by nuclear magnetic resonance (NMR) were surveyed for all the essential metal complexes and many non-essential metal complexes. The various methods used to study each metal ion are presented together with examples of recent research. Many of these metal systems have been individually reviewed and this current overview of NMR studies of metallopeptide complexes aims to provide a basis for inspiration from structural studies and methodology applied in the field.

Original languageAmerican English
Article number15957
JournalInternational Journal of Molecular Sciences
Volume23
Issue number24
DOIs
StatePublished - Dec 2022

Bibliographical note

Publisher Copyright:
© 2022 by the author.

Keywords

  • NMR
  • metallopeptides
  • peptide chelates
  • peptide structure
  • peptides
  • structural NMR

Fingerprint

Dive into the research topics of 'Studying Peptide-Metal Ion Complex Structures by Solution-State NMR'. Together they form a unique fingerprint.

Cite this