Gordon, D. Benjamin and Marshall, Shannon A. and Mayo, Stephen L. (1999) Energy functions for protein design. Current Opinion in Structural Biology, 9 (4). pp. 509-513. ISSN 0959-440X http://resolver.caltech.edu/CaltechAUTHORS:20110621-154505395
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Recent successes in protein design have illustrated the promise of computational approaches. These methods rely on energy expressions to evaluate the quality of different amino acid sequences for target protein structures. The force fields optimized for design differ from those typically used in molecular mechanics and molecular dynamics calculations.
|Additional Information:||© 1999 Elsevier Science Ltd. Available online 22 September 1999. We wish to thank AG Street for helpful comments on the manuscript. This work was supported by the Howard Hughes Medical Institute (SLM), the Helen G and Arthur McCallum Foundation (DBG), a National Institutes of Health NRSA training grant and the Caltech Initiative in Computational Molecular Biology program, awarded by the Burroughs Wellcome Fund (SAM).|
|Subject Keywords:||Protein Engineering, Hydrogen Bonding, Models: Molecular, Solubility, Entropy, Chemistry: Physical, Physicochemical Phenomena, Computer Simulation, Static Electricity, Energy Metabolism, Drug Design, Models: Chemical|
|Official Citation:||D Benjamin Gordon, Shannon A Marshall, Stephen L Mayot, Energy functions for protein design, Current Opinion in Structural Biology, Volume 9, Issue 4, August 1999, Pages 509-513, ISSN 0959-440X, DOI: 10.1016/S0959-440X(99)80072-4. (http://www.sciencedirect.com/science/article/pii/S0959440X99800724)|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Benjamin Perez|
|Deposited On:||21 Jun 2011 23:16|
|Last Modified:||21 Jun 2011 23:16|
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