Open Access. Powered by Scholars. Published by Universities.®

Other Chemistry Commons

Open Access. Powered by Scholars. Published by Universities.®

2017

University of Massachusetts Amherst

Articles 1 - 1 of 1

Full-Text Articles in Other Chemistry

How The E. Coli Hsp70 Molecular Chaperone, Dnak, Binds A Client Protein, Joseph Tilitsky Oct 2017

How The E. Coli Hsp70 Molecular Chaperone, Dnak, Binds A Client Protein, Joseph Tilitsky

Masters Theses

Protein folding is essential for all cellular life. While some proteins are able to reach their folded state reliably using nothing but their amino acid sequence, a great number of essential proteins are unable to do so without the aid of molecular chaperones. One family of molecular chaperone, the Hsp70 family, is found in virtually all cell types and across all domains of life. Certain to the function of Hsp70s are how they bind their client proteins. Substantial effort has been expended to study how Hsp70s work on model peptides as a substrate mimic, but relatively little work has been …