Influence of Temperature on the Dynamic Structures of Psychrophilic Small Heat Shock Proteins
Abstract
Inappropriate aggregation of peptides and proteins is a major concern for biotechnology and is also associated with several major human pathological conditions. The goal of this project is to develop a robust method for refolding proteins and peptides by adapting novel protein salvage pathways from extremophiles to operate under mild conditions. In prior studies, we have shown that the chaperones from extremophiles are exceptionally stable and versatile, reflecting their role in folding and salvaging proteins under extreme conditions. The remarkably thermostable small Heat Shock Protein from the psychrotolerant archaeon Methanococcoides burtonii is our first choice for a "holdase" chaperone. This crystallin-like chaperone is stable from 15-55-deg C, and maintains aggregation-prone target proteins in the soluble state, without denaturants. In addition to applications of this pathway to recombinant proteins in solution and during expression in vivo, we propose to immobilize the chaperones to form a chaperone matrix.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 27, 2010
- Accession Number
- ADA518387
Entities
People
- Frank T. Robb
- Pongpan Laksanalamai
Organizations
- University of Maryland, Baltimore