These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Turn residues in beta-hairpin peptides as points for covalent modification.
    Author: Cooper WJ, Waters ML.
    Journal: Org Lett; 2005 Sep 01; 7(18):3825-8. PubMed ID: 16119908.
    Abstract:
    Beta-turns are important sites for protein-protein and protein-peptide interactions, but little research has explored synthetic modifications of turn residue side-chains in a beta-hairpin peptide. To this end, beta-hairpin peptides were synthesized containing the type I' turn sequence Val-Asn-Gly-Lys with modifications at Asn and Lys. We found that these variations impose a small penalty, demonstrating that beta-turns are capable of displaying a range of functionality, which may be exploited for biomolecular recognition and medicinal applications. [structure: see text]
    [Abstract] [Full Text] [Related] [New Search]