The calcium-dependent interactions of p53 and other intrinsically disordered peptides with members of the S100 protein family.

Authors
Wafer, Lucas N. R.
ORCID
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Other Contributors
Makhatadze, George I.
García, Angel E.
McCallum, Scott A.
Barquera, Blanca L.
Karande, Pankaj
Issue Date
2013-08
Keywords
Biology
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
Understanding the molecular recognition that occurs during protein-protein interactions is one of the fundamental goals of biochemistry. These interactions are of particular interest because of their role in signal transduction and regulation. Recently, it has become evident that many of these interactions are the result of large, globular proteins recognizing a short amino acid sequence in, or a structural motif on, their partner proteins. In some cases, the binding epitope has been shown to be as small as a few residues, such as binding of the SH2 or SH3 domains. This discovery was somewhat surprising considering the large quantity of solvent-accessible surface area available for binding on most proteins and has raised a number of key questions. How do small sequences encode binding specificity? How are homologous proteins, with similar sequences and tertiary structures, able to differentiate between binding partners? How do a sequence and its structure influence the thermodynamic and kinetic modes of binding?
Description
August 2013
School of Science
Department
Dept. of Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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