Ontology highlight
ABSTRACT:
SUBMITTER: Tennyson RL
PROVIDER: S-EPMC6013031 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Tennyson Rachel L RL Walker Susanne N SN Ikeda Terumasa T Harris Reuben S RS Kennan Alan J AJ McNaughton Brian R BR
Chembiochem : a European journal of chemical biology 20160830 20
The size, functional group diversity and three-dimensional structure of proteins often allow these biomolecules to bind disease-relevant structures that challenge or evade small-molecule discovery. Additionally, folded proteins are often much more stable in biologically relevant environments compared to their peptide counterparts. We recently showed that helix-grafted display-extensive resurfacing and elongation of an existing solvent-exposed helix in a pleckstrin homology (PH) domain-led to a n ...[more]