Ontology highlight
ABSTRACT:
SUBMITTER: Baker EG
PROVIDER: S-EPMC4668598 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Nature chemical biology 20150209 3
The noncovalent forces that stabilize protein structures are not fully understood. One way to address this is to study equilibria between unfolded states and α-helices in peptides. Electrostatic forces-which include interactions between side chains, the backbone and side chains, and side chains and the helix macrodipole-are believed to contribute to these equilibria. Here we probe these interactions experimentally using designed peptides. We find that both terminal backbone-side chain and certai ...[more]