Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues.

ABSTRACT: Flory's random coil model assumes that conformational fluctuations of amino acid residues in unfolded poly(oligo)peptides and proteins are uncorrelated (isolated pair hypothesis, IPH). This implies that conformational energies, entropies and solvation free energies are all additive. Nearly 25 years ago, analyses of coil libraries cast some doubt on this notion, in that they revealed that aromatic, but also β-branched side chains, could change the ³J(H^NH^Cα) coupling of their neighbors. Since then, multiple bioinformatical, computational and experimental studies have revealed that conformational propensities of amino acids in unfolded peptides and proteins depend on their nearest neighbors. We used recently reported and newly obtained Ramachandran plots of te

SUBMITTER: Schweitzer-Stenner R 

PROVIDER: S-EPMC9138747 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature