Computational design of second-site suppressor mutations at protein-protein interfaces
نویسندگان
چکیده
منابع مشابه
Second-site suppressor mutations of inactivating substitutions at gly247 of the tetracycline efflux protein, Tet(B).
An Asp or Asn substitution for Gly247 in transmembrane helix 8 (TM-8) of Tet(B), the tetracycline efflux protein, eliminated tetracycline resistance. Second site suppressor mutations which partially restored resistance were located in TM-5, -8, -10, or -11 or in cytoplasmic loop 8-9 or loop 10-11. These results indicate physical proximity or functional relationships between TM-8 and these other...
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Manipulations of PPIs (protein-protein interactions) are important for many biological applications such as synthetic biology and drug design. Combinatorial methods have been traditionally used for such manipulations, failing, however, to explain the effects achieved. We developed a computational method for prediction of changes in free energy of binding due to mutation that bring about deeper ...
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BACKGROUND Few existing protein-protein interface design methods allow for extensive backbone rearrangements during the design process. There is also a dichotomy between redesign methods, which take advantage of the native interface, and de novo methods, which produce novel binders. METHODOLOGY Here, we propose a new method for designing novel protein reagents that combines advantages of rede...
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ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Bioinformatics
سال: 2009
ISSN: 0887-3585
DOI: 10.1002/prot.22631