Quantification of Drive-Response Relationships Between Residues During Protein Folding.

ABSTRACT: Mutual correlation and cooperativity are commonly used to describe residue-residue interactions in protein folding/function. However, these metrics do not provide any information on the causality relationships between residues. Such drive-response relationships are poorly studied in protein folding/function and difficult to measure experimentally due to technical limitations. In this study, using the information theory transfer entropy (TE) that provides a direct measurement of causality between two times series, we have quantified the drive-response relationships between residues in the folding/unfolding processes of four small proteins generated by molecular dynamics simulations. Instead of using a time-averaged single TE value, the time-dependent TE is measured with the Q-scores based o

SUBMITTER: Qi Y 

PROVIDER: S-EPMC3819712 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature