Markov models of amino acid substitution to study proteins with intrinsically disordered regions.

ABSTRACT:

Background

Intrinsically disordered proteins (IDPs) or proteins with disordered regions (IDRs) do not have a well-defined tertiary structure, but perform a multitude of functions, often relying on their native disorder to achieve the binding flexibility through changing to alternative conformations. Intrinsic disorder is frequently found in all three kingdoms of life, and may occur in short stretches or span whole proteins. To date most studies contrasting the differences between ordered and disordered proteins focused on simple summary statistics. Here, we propose an evolutionary approach to study IDPs, and contrast patterns specific to ordered protein regions and the corresponding IDRs.

Results

Two empirical Markov models of amino acid substitutions were estimated, based o

SUBMITTER: Szalkowski AM 

PROVIDER: S-EPMC3103576 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature