The Hsp70 heat-shock proteins constitute a family of chaperones recognized for their plethora of roles in the domain of protein repair, agglomerate prevention, and folding assistance. The mechanistic details of their function have not yet been clearly delineated, which owing to their ubiquitous nature and potential as drug targets in agglomerate-based disease, renders the topic one of intense research. The present study employed canonical molecular dynamics in simulations modeling the Nucleotide Binding Domain (NBD) of the chaperone, where emphasis was placed on understanding the effects induced by the binding of ADP or ATP on the behavior of the NBD. Essential Dynamics analysis was conducted as a means of deconvoluting the major and characteristic motions associated with the various states of nucleotide binding, in addition to the tendencies of the protein in its nucleotide-free state. Connections within and insight into Hsp70 structure-function were then drawn.

Molecular dynamics of the Hsp70 chaperone's Nucleotide Binding Domain: Understanding nucleotide binding and structure-function relationships

245th National Meeting (2013)

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