Beyond basins: φ,ψ preferences of a residue depend heavily on the φ,ψ values of its neighbors.

ABSTRACT: The Ramachandran plot distributions of nonglycine residues from experimentally determined structures are routinely described as grouping into one of six major basins: β, PII , α, αL , ξ and γ'. Recent work describing the most common conformations adopted by pairs of residues in folded proteins [i.e., (φ,ψ)2 -motifs] showed that commonly described major basins are not true single thermodynamic basins, but are composed of distinct subregions that are associated with various conformations of either the preceding or following neighbor residue. Here, as documentation of the extent to which the conformational preferences of a central residue are influenced by the conformations of its two neighbors, we present a set of φ,ψ-plots that are delimited simultaneously by the φ,ψ-angles of its neighbori

SUBMITTER: Hollingsworth SA 

PROVIDER: S-EPMC5338229 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature