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Proline Isomerization and Protein Folding

  • Christy MacKinnon
  • Sudha Veeraraghavan
  • Isabelle Kreider
  • Michael J. Allen
  • John R. Liggins
  • Barry T. Nall
Part of the Industry-University Cooperative Chemistry Program Symposia book series (IUCC)

Abstract

A reaction as complex as folding of a protein must involve a variety specific chemical processes. Hydrogen bonds and salt bridges are formed, and perhaps broken and interchanged. Solvent-induced hydrophobic associations may occur, or even a general hydrophobic collapse of the polypeptide to a less than fully ordered “globule”. Polypeptide chains might become entangled with each other or with other chains and have to extricate themselves prior to further folding. Intricate shapes and structures may be constructed only to partially or fully unravel on transformation into other more stable forms. The objective of much experimental work on the process of folding has been to obtain direct evidence for some of these expectations. This has been a major challenge since many aspects of folding, rather than having the expected complexity, are, instead, well described by the simplest of chemical mechanisms: a two state process.

Keywords

Mutant Protein Slow Phasis Folding Intermediate Peptidyl Prolyl Isomerase Horse Cytochrome 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Christy MacKinnon
    • 1
  • Sudha Veeraraghavan
    • 1
  • Isabelle Kreider
    • 1
  • Michael J. Allen
    • 1
  • John R. Liggins
    • 1
  • Barry T. Nall
    • 1
  1. 1.Department of BiochemistryUniversity of Texas Health Science CenterSan AntonioUSA

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