Ontology highlight
ABSTRACT:
SUBMITTER: Kasperkiewicz P
PROVIDER: S-EPMC3932852 | biostudies-other | 2014 Feb
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 20140203 7
The exploration of protease substrate specificity is generally restricted to naturally occurring amino acids, limiting the degree of conformational space that can be surveyed. We substantially enhanced this by incorporating 102 unnatural amino acids to explore the S1-S4 pockets of human neutrophil elastase. This approach provides hybrid natural and unnatural amino acid sequences, and thus we termed it the Hybrid Combinatorial Substrate Library. Library results were validated by the synthesis of ...[more]