Studying protein folding cooperativity with pressure perturbation
Authors
Zhang, Yi
ORCID
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Other Contributors
Royer, Catherine Ann
Colón, Wilfredo
Linhardt, Robert J.
Tessier, Peter M.
Wang, Chunyu
Colón, Wilfredo
Linhardt, Robert J.
Tessier, Peter M.
Wang, Chunyu
Issue Date
2017-05
Keywords
Chemistry
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
protein. The C-terminal domain of the ribosomal protein L9 (CTL9) is a small globular protein. Pressure and temperature dependent NMR revealed significant deviations from two-state behavior for CTL9, with its hydrophobic core selectively destabilized by increasing temperature. Yet the I98A mutation in the core resulted in highly cooperative pressure unfolding. These observations indicate that local stability, as opposed to long-range interactions, determines folding cooperativity.
Description
May 2017
School of Science
School of Science
Department
Dept. of Chemistry and Chemical Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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