Conformational Entropy of Intrinsically Disordered Proteins from Amino Acid Triads.

ABSTRACT: This work quantitatively characterizes intrinsic disorder in proteins in terms of sequence composition and backbone conformational entropy. Analysis of the normalized relative composition of the amino acid triads highlights a distinct boundary between globular and disordered proteins. The conformational entropy is calculated from the dihedral angles of the middle amino acid in the amino acid triad for the conformational ensemble of the globular, partially and completely disordered proteins relative to the non-redundant database. Both Monte Carlo (MC) and Molecular Dynamics (MD) simulations are used to characterize the conformational ensemble of the representative proteins of each group. The results show that the globular proteins span approximately half of the allowed conformational states

SUBMITTER: Baruah A 

PROVIDER: S-EPMC4490338 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature