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The effect of proline cistrans isomerization on p53MDM2 binding.

Proline is unique in that it is the only amino acid that adopts both cis and trans conformations in proteins. In spite of the importance of proline isomerization as a molecular switch in proteins, the effect on protein binding has not been thoroughly investigated, especially for intrinsically disordered proteins (IDPs). In this study, a potential of mean force method was used to calculate the absolute binding affinities for the disordered p53 and MDM2 when the proline in p53 is in both cis and trans conformations. To obtain converged affinity results it was necessary to apply conformational, axial, and orientational restraints to the protein internal coordinates. Our results give insight into how isomerization of a proline affects binding of an IDP to a structured protein.

Yingqian Ada Zhan and F. Marty Ytreberg

University of Idaho

ytreberg@uidaho.edu

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Title Annotation:56TH ANNUAL SYMPOSIUM OF THE IDAHO ACADEMY OF SCIENCE: THEME: ENERGY, MATERIALS, AND NANOTECHNOLOGY
Author:Zhan, Yingqian Ada; Ytreberg, F. Marty
Publication:Journal of the Idaho Academy of Science
Article Type:Abstract
Geographic Code:1USA
Date:Dec 1, 2014
Words:137
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