Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study.

ABSTRACT: Technical strategies like amino acid substitution and residue modification have been widely used to characterize the importance of key amino acids and the role that each residue plays in the structural and functional properties of protein molecules. However, there is no systematic approach to assess the impact of the substituted/modified amino acids on the conformational dynamics of proteins. In this investigation to clarify the effects of residue modifications on the structural dynamics of human prion protein (PrP), a comparative molecular dynamics simulation study on the native and the amino acid-substituted analog at position 208 of PrP has been performed. It is believed that Arginine to Histidine mutation at position 208 is responsible for the structural transition of the native form o

SUBMITTER: Bamdad K 

PROVIDER: S-EPMC4464497 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature