Decoding the components of dynamics in three-domain proteins.

ABSTRACT: In this study, we examine the feasibility and limitations of describing the motional behavior of three-domain proteins in which the domains are linearly connected. In addition to attempting the determination of the internal and overall reorientational correlation times, we investigate the existence of correlations in the motions between the three domains. Since in linearly arranged three-domain proteins, there are typically no experimental data that can directly report on motional correlation between the first and the third domain, we address this question by dynamics simulations. Two limiting cases occur: (1) for weak repulsive potentials and (2) when strong repulsive potentials are applied between sequential domains. The motions of the terminal domains become correlated in the case of st

SUBMITTER: Maciejewski M 

PROVIDER: S-EPMC4181349 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature