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.
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© 1989 Plenum Press, New York
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McCammon, J.A., Wong, C.F., Lybrand, T.P. (1989). Protein Stability and Function. In: Fasman, G.D. (eds) Prediction of Protein Structure and the Principles of Protein Conformation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1571-1_4
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DOI: https://doi.org/10.1007/978-1-4613-1571-1_4
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