Ontology highlight
ABSTRACT:
SUBMITTER: Shoulders MD
PROVIDER: S-EPMC2818912 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Shoulders Matthew D MD Satyshur Kenneth A KA Forest Katrina T KT Raines Ronald T RT
Proceedings of the National Academy of Sciences of the United States of America 20091231 2
Preorganization is shown to endow a protein with extraordinary conformational stability. This preorganization is achieved by installing side-chain substituents that impose stereoelectronic and steric effects that restrict main-chain torsion angles. Replacing proline residues in (ProProGly)(7) collagen strands with 4-fluoroproline and 4-methylproline leads to the most stable known triple helices, having T ( m ) values that are increased by > 50 degrees C. Differential scanning calorimetry data in ...[more]