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Article
Native State Proline Isomerization:  An Intrinsic Molecular Switch
Biochemistry
  • Amy H. Andreotti, Iowa State University
Document Type
Article
Publication Version
Published Version
Publication Date
7-1-2003
DOI
10.1021/bi0350710
Abstract
Exquisite control of biological function is achieved via tight regulation of the catalytic and binding activities of cellular proteins. The mechanistic details of protein regulation vary from targeted chemical modification of amino acid side chains (1) to the quite drastic global unfolding of an entire polypeptide chain (2). Peptidyl prolyl cis/trans isomerization is emerging as a potentially general mechanism for the control of protein function (3). While most structures of native, folded proteins reveal peptidyl-prolyl imide bonds that adopt either the cis or trans conformation, there are a growing number of folded proteins that exhibit conformational heterogeneity about one or more peptidyl-prolyl bonds. Unlike covalent modification or global unfolding, proline isomerization is an intrinsic conformational exchange process that has the potential to direct ligand recognition and to control protein activity within the confines of the native state.
Comments

Reprinted (adapted) with permission from Biochemistry 42 (2003), 9515, doi:10.1021/bi0350710. Copyright 2003 American Chemical Society.

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Copyright Owner
American Chemical Society
Language
en
File Format
application/pdf
Citation Information
Amy H. Andreotti. "Native State Proline Isomerization:  An Intrinsic Molecular Switch" Biochemistry Vol. 42 Iss. 32 (2003) p. 9515 - 9524
Available at: http://works.bepress.com/amy_andreotti/4/