Copper-induced spectroscopic and structural changes in short peptides derived from azurin.
Azurin
Copper-binding
Ligand-binding
Metalloprotein
Peptide mimics
Protein mimics
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 07 2020
15 07 2020
Historique:
received:
24
02
2020
revised:
07
04
2020
accepted:
21
04
2020
pubmed:
29
4
2020
medline:
3
10
2020
entrez:
29
4
2020
Statut:
ppublish
Résumé
The active sites of metalloproteins may be mimicked by designing peptides that bind to their respective metal ions. Studying the binding of protein ligands to metal ions along with the associated structural changes is important in understanding metal uptake, transport and electron transfer functions of proteins. Copper-binding metalloprotein azurin is a 128-residue electron transfer protein with a redox-active copper cofactor. Here, we report the copper-binding associated spectroscopic and structural properties of peptide loops (11 and 13 residues) from the copper-binding site of azurin. These peptides develop a β-turn upon copper-binding with a 1:1 Cu
Identifiants
pubmed: 32343975
pii: S0003-9861(20)30397-0
doi: 10.1016/j.abb.2020.108388
pii:
doi:
Substances chimiques
Peptide Fragments
0
Azurin
12284-43-4
Copper
789U1901C5
Tryptophan
8DUH1N11BX
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108388Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.