Ontology highlight
ABSTRACT:
SUBMITTER: Creamer TP
PROVIDER: S-EPMC2143171 | biostudies-other | 1995 Jul
REPOSITORIES: biostudies-other
Protein science : a publication of the Protein Society 19950701 7
The thermodynamic basis of helix stability in peptides and proteins is a topic of considerable interest. Accordingly, we have computed the interactions between side chains of all hydrophobic residue pairs and selected triples in a model helix, using Boltzmann-weighted exhaustive modeling. Specifically, all possible pairs from the set Ala, Cys, His, Ile, Leu, Met, Phe, Trp, Tyr, and Val were modeled at spacings of (i, i + 2), (i, i + 3), and (i, i + 4) in the central turn of a model poly-alanyl a ...[more]