Discovering conformational sub-states relevant to protein function.

ABSTRACT:

Background

Internal motions enable proteins to explore a range of conformations, even in the vicinity of native state. The role of conformational fluctuations in the designated function of a protein is widely debated. Emerging evidence suggests that sub-groups within the range of conformations (or sub-states) contain properties that may be functionally relevant. However, low populations in these sub-states and the transient nature of conformational transitions between these sub-states present significant challenges for their identification and characterization.

Methods and findings

To overcome these challenges we have developed a new computational technique, quasi-anharmonic analysis (QAA). QAA utilizes higher-order statistics of protein motions to identify sub-states in the

SUBMITTER: Ramanathan A 

PROVIDER: S-EPMC3030567 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature