Computational protein design engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins推荐.pdf
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Computational protein design engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins推荐
NIH Public Access
Author Manuscript
Curr Opin Chem Biol. Author manuscript; available in PMC 2014 July 01.
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Published in final edited form as:
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Curr Opin Chem Biol. 2011 June ; 15(3): 452–457. doi:10.1016/j.cbpa.2011.03.014.
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u Computational protein design: engineering molecular diversity,
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r nonnatural enzymes, nonbiological cofactor complexes, and
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a membrane proteins
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c Jeffery G Saven
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p Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA
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19104
Abstract
Computational and theoretical methods are advancing protein design as a means to create and
investigate proteins. Such efforts further our capacity to control, design and understand
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biomolecular structure, sequence and function. Herein, the focus is on some recent applications
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that involve using theoretical and computational methods to guide the design of protein sequence
A ensembles, new enzymes, proteins with novel cofactors, and membrane proteins.
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o Overview
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a Nature’s proteins fold to yield a variety of functionalities, including self-assembly,
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u enzymatic catalysis and highly selective molecular recognition. The structure and function
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c of proteins can potentially be specified through the careful selection of sequence. During the
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p course of evolution, Nature varies the physical and chemical properties of a protein through
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mutation and variation of sequence to
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