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Determination of Dynamical Conservation in Human Cyclophilin Isoforms

Among the peptidyl prolyl isomerases, the Cyclophilin family of proteins has been linked to various cellular activities such as regulation of homeostasis, mitochondrial permeability, and cell death. Their functionality spans throughout the cell and throughout all cell types as different isoforms. Previous studies done on Cyclophilin A revealed an interesting contact ensemble when bound to a substrate. Because of the similarity of CypA to its homologues, it is believed that they too will exhibit the same contact dynamics. We have defined the dynamics of cyclophilin isoforms through Molecular Dynamics simulations and determined their contact dynamics, characterizing their contact ensembles, and their relative dynamical conservation to each other.

Identiferoai:union.ndltd.org:GEORGIA/oai:scholarworks.gsu.edu:chemistry_theses-1110
Date08 August 2017
CreatorsVu, Phuoc Jake D.
PublisherScholarWorks @ Georgia State University
Source SetsGeorgia State University
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceChemistry Theses

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