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

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.

Saved in:
Bibliographic Details
Main Authors: Julia C. Heiby, Benedikt Goretzki, Christopher M. Johnson, Ute A. Hellmich, Hannes Neuweiler
Format: article
Language:EN
Published: Nature Portfolio 2019
Subjects:
Q
Online Access:https://doaj.org/article/cbb044ff25df467b8fda4b6d45554c9a
Tags: Add Tag
No Tags, Be the first to tag this record!