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Article
Protein Stability and Function
Prediction of Protein Structure and the Principles of Protein Conformation (1989)
  • J. Andrew McCammon, University of Houston
  • Chung F. Wong, University of Houston
  • Terry P. Lybrand, University of Houston
Abstract
The convergence of several lines of development in chemistry and molecular biology has created major new needs and opportunities for theoretical studies of proteins. The traditional approaches of organic synthesis have been supplemented by methods for automated chemical synthesis and genetic engineering that allow the preparation of a wide variety of polypeptides, specifically altered enzymes, and other complex molecules. The choice of molecules to be synthesis for a given application is increasingly guided by structural information in addition to traditional methods such as chemical intuition and empirical correlation (quantitative structure-activity relationships, or QSAR). X-ray area detectors and new methods in NMR spectroscopy, combined with the improvements in our ability to synthesize and purify samples, are increasingly the rate at which high-resolution structures to proteins are becoming available.
Keywords
  • Kcal Mole,
  • Protein Stability,
  • Free Energy Change,
  • Thermodynamic Cycle,
  • Relative Free Energy
Disciplines
Publication Date
January 1, 1989
DOI
10.1007/978-1-4613-1571-1_4
Citation Information
J. Andrew McCammon, Chung F. Wong and Terry P. Lybrand. "Protein Stability and Function" Prediction of Protein Structure and the Principles of Protein Conformation (1989) p. 149 - 159
Available at: http://works.bepress.com/chung-wong/68/