Ontology highlight
ABSTRACT:
SUBMITTER: Kolbel K
PROVIDER: S-EPMC6289508 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Kölbel Knut K Warnke Stephan S Seo Jongcheol J von Helden Gert G Moretti Rocco R Meiler Jens J Pagel Kevin K Sinz Andrea A
ChemistrySelect 20160819 13
So-called super-secondary structures such as the β-hairpin, studied here, form an intermediate hierarchy between secondary and tertiary structures of proteins. Their sequence-derived 'pure' peptide backbone conformation is combined with 'remote' interstrand or interresidue contacts reminiscent of the 3D-structure of full-length proteins. This renders them ideally suited for studying potential nucleation sites of protein folding reactions as well as intermolecular interactions. But β-hairpins do ...[more]