Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
oleh: Julia C. Heiby, Benedikt Goretzki, Christopher M. Johnson, Ute A. Hellmich, Hannes Neuweiler
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2019-09-01 |
Deskripsi
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.