Characterizing Protein Folding Transition States Using Psi-analysis.
From: Department of Biochemistry and Molecular Biology, University of Chicago, IL, USA.
Methods in molecular biology (Clifton, N.J.)
- Publish Date: 2007
- ISSN: 1064-3745
- Volume: 350
- Issue:
- Pages: 83-104
- Medium: Print
- Language: English
- Citation (JAMA): Pandit Adarsh D, Krantz Bryan A, Dothager Robin S, et al. Characterizing Protein Folding Transition States Using Psi-analysis.. Methods Mol. Biol. 2007;350:83-104
Abstract
We discuss the implementation of Psi-analysis for the structural characterization of protein folding transition states. In Psi-analysis, engineered bi-histidine metal ion binding sites are introduced at surface positions to stabilize secondary and tertiary structures. The addition of metal ions stabilizes the interaction between the two known histidines in a continuous fashion. Measuring the ratio of transition state stabilization to that of the native state provides information about the presence of the metal binding site in the transition state. Psi-Analysis uses noninvasive surface mutations and does not require specialized equipment, so it can be readily applied to characterize the folding of many proteins. As a result, this method can provide a wealth of high-resolution quantitative data for comparison with theoretical folding simulations. Additionally, investigations of other biological processes also may utilize metal binding sites and Psi-analysis to detect conformational events during catalysis, assembly, and function.
Mesh Headings (Keywords): Binding Sites, Histidine, Kinetics, Metals, Models, Molecular, Protein Conformation, Protein Engineering, Protein Folding, Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16957319
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