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

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 det...

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Autor principal: Shalev, Deborah E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9782655/
https://www.ncbi.nlm.nih.gov/pubmed/36555599
http://dx.doi.org/10.3390/ijms232415957
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author Shalev, Deborah E.
author_facet Shalev, Deborah E.
author_sort Shalev, Deborah E.
collection PubMed
description 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.
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spelling pubmed-97826552022-12-24 Studying Peptide-Metal Ion Complex Structures by Solution-State NMR Shalev, Deborah E. Int J Mol Sci Review 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. MDPI 2022-12-15 /pmc/articles/PMC9782655/ /pubmed/36555599 http://dx.doi.org/10.3390/ijms232415957 Text en © 2022 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Shalev, Deborah E.
Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title_full Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title_fullStr Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title_full_unstemmed Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title_short Studying Peptide-Metal Ion Complex Structures by Solution-State NMR
title_sort studying peptide-metal ion complex structures by solution-state nmr
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9782655/
https://www.ncbi.nlm.nih.gov/pubmed/36555599
http://dx.doi.org/10.3390/ijms232415957
work_keys_str_mv AT shalevdeborahe studyingpeptidemetalioncomplexstructuresbysolutionstatenmr