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.

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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

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Hsp70 Conformational Plasticity Allows for Expansive Chaperone Role

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