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High-resolution crystal structure of a lasso peptide

Nar, H. and Schmid, A. and Puder, C. and Potterat, O.. (2010) High-resolution crystal structure of a lasso peptide. ChemMedChem, Vol. 5, H. 10. pp. 1689-1692.

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Official URL: http://edoc.unibas.ch/dok/A5839905

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Abstract

Lasso peptides are a group of a growing class of bioactive peptides of microbial origin. The first crystal structure of a member of this family, the glucagon receptor antagonist BI-32169, shows that the fold is built predominantly by regular secondary structural elements and a tight network of hydrogen bonds that are partially shielded from solvent by hydrophobic amino acid side chains. This results in an extraordinary stable structure that is resistant to thermal unfolding or proteolytic digestion, which facilitates its biological function.
Faculties and Departments:05 Faculty of Science > Departement Pharmazeutische Wissenschaften > Pharmazie > Pharmazeutische Biologie (Hamburger)
UniBasel Contributors:Potterat, Olivier
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Wiley-VCH
ISSN:1860-7179
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Sep 2012 07:17
Deposited On:14 Sep 2012 06:37

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