Abstract
Modified ubiquitin sequences, each completed with a His tag and a TEV cleavage site, were designed to enhance the expression of protein/peptide targets. With this new system we have been able to characterize several peptide-protein interactions by ITC and by NMR and CD spectroscopic methods, including the interactions of LIR domains with autophagy modifiers.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
Expressed Sequence Tags / chemistry*
-
Genetic Vectors / genetics
-
Models, Molecular
-
Molecular Sequence Data
-
Nuclear Magnetic Resonance, Biomolecular / methods
-
Protein Biosynthesis
-
Protein Structure, Tertiary
-
Proteins / chemistry*
-
Proteins / genetics
-
Recombinant Fusion Proteins / biosynthesis*
-
Recombinant Fusion Proteins / chemistry*
-
Recombinant Fusion Proteins / genetics
-
Ubiquitin / genetics
-
Ubiquitin / metabolism
Substances
-
Proteins
-
Recombinant Fusion Proteins
-
Ubiquitin