Computational protein design engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins推荐.pdfVIP

NIH Public Access Author Manuscript Curr Opin Chem Biol. Author manuscript; available in PMC 2014 July 01. N Published in final edited form as: I H Curr Opin Chem Biol. 2011 June ; 15(3): 452–457. doi:10.1016/j.cbpa.2011.03.014. - P A A u Computational protein design: engineering molecular diversity, t h o r nonnatural enzymes, nonbiological cofactor complexes, and M a membrane proteins n u s c Jeffery G Saven r i p Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA t 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 N I H biomolecular structure, sequence and function. Herein, the focus is on some recent applications - P 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. A u t h o Overview r M a Nature’s proteins fold to yield a variety of functionalities, including self-assembly, n u enzymatic catalysis and highly selective molecular recognition. The structure and function s c of proteins can potentially be specified through the careful selection of sequence. During the r i p course of evolution, Nature varies the physical and chemical properties of a protein through t mutation and variation of sequence to