Profiling primary protease specificity by peptide synthesis on a solid support
Doeze, R H P and Maltman, B A and Egan, C L and Ulijn, R V and Flitsch, S L (2004) Profiling primary protease specificity by peptide synthesis on a solid support. Agewandte Chemie-International Edition, 43 (24). pp. 3138-3141. ISSN 1433-7851
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Abstract
Reverse screening: A greatly simplified primary screening of protease specificity has been achieved by monitoring the fluorescence during the protease-catalyzed coupling of amino acids instead of peptide hydrolysis on a solid support (see picture, AA=amino acid). This approach paves the way for flexible, rapid, high-throughput identification and characterization of proteases without the need for expensively labeled peptide arrays.
Creators(s): |
Doeze, R H P, Maltman, B A, Egan, C L, Ulijn, R V ![]() | Item type: | Article |
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ID code: | 43940 |
Keywords: | profiling, primary protease specificity, peptide synthesis, solid support, hydrolysis, substrate specificity, enzymes, fluorescent probe, high-throughput screening, Chemistry, Pharmacy and materia medica, Chemistry(all), Catalysis |
Subjects: | Science > Chemistry Medicine > Pharmacy and materia medica |
Department: | Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Faculty of Science > Pure and Applied Chemistry |
Depositing user: | Pure Administrator |
Date deposited: | 30 May 2013 11:23 |
Last modified: | 20 Jan 2021 20:42 |
URI: | https://strathprints.strath.ac.uk/id/eprint/43940 |
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