D.U.Quark
Abstract
The Hsp70 system is an essential component of chaperone activity in many organisms. Hsp70 functions include: protein folding, aggregation prevention, trafficking, and enzyme regulation. Hsp70’s ability to bind such a vast array of substrates suggests wide range of conformational plasticity. By utilizing a single mode optical tweezers technique, Mashaghi1 et al., confirms previous theories Hsp70 binds and stabilizes extended peptide segments but also partially folded and near-native protein.
Instructor
Dr. O'Donnell
First Page
29
Last Page
34
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Recommended Citation
Bean, M. (2017). Hsp70 Conformational Plasticity Allows for Expansive Chaperone Role. D.U.Quark, 2 (1). Retrieved from https://dsc.duq.edu/duquark/vol2/iss1/4