Hydrophobic residues of melittin mediate its binding to αA−crystallin
Author:
Affiliation:
1. Department of Chemistry, University at AlbanyState University of New York Albany New York
Funder
National Institute of General Medical Sciences
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3792
Reference78 articles.
1. Alpha-crystallin
2. Structure and function of α-crystallins: Traversing from in vitro to in vivo
3. Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins
4. Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
5. Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB
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