Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

Autor: Julia C. Heiby, Benedikt Goretzki, Christopher M. Johnson, Ute A. Hellmich, Hannes Neuweiler
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-019-12365-5
Popis: Spider silk is of interest in material science research. Here the authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.
Databáze: Directory of Open Access Journals