Ontology highlight
ABSTRACT:
SUBMITTER: Berkholz DS
PROVIDER: S-EPMC2810841 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
Berkholz Donald S DS Shapovalov Maxim V MV Dunbrack Roland L RL Karplus P Andrew PA
Structure (London, England : 1993) 20091001 10
Protein structure determination and predictive modeling have long been guided by the paradigm that the peptide backbone has a single, context-independent ideal geometry. Both quantum-mechanics calculations and empirical analyses have shown this is an incorrect simplification in that backbone covalent geometry actually varies systematically as a function of the phi and Psi backbone dihedral angles. Here, we use a nonredundant set of ultrahigh-resolution protein structures to define these conforma ...[more]