Sequence optimization and designability of enzyme active sites
نویسندگان
چکیده
منابع مشابه
Sequence optimization and designability of enzyme active sites.
We recently found that many residues in enzyme active sites can be computationally predicted by the optimization of scoring functions based on substrate binding affinity, subject to constraints on the geometry of catalytic residues and protein stability. Here, we explore the generality of this surprising observation. First, the impact of hydrogen-bonding networks necessary for catalysis on the ...
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Enzymes are critical in many cellular signaling cascades. With many enzyme structures being solved, there is an increasing need to develop an automated method for identifying their active sites. However, given the atomic coordinates of an enzyme molecule, how can we predict its active site? This is a vitally important problem because the core of an enzyme molecule is its active site from the vi...
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The high resolution refined structures of 23 enzymes were analyzed to determine the properties of amino acids involved in active site regions. These regions were found to be rich in G-X-Y or Y-X-G oligopeptides, where X and Y are polar and non-polar residues, respectively, that are small and with low polarity. Other regions of the enzyme molecules have significantly fewer of these sequences. Th...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2005
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0505397102