【摘 要】
：
Using a combination of multinuclear NMR spectroscopy,high resolution X-ray crystallography and computational chemistry we are able to examine the conformational behaviour of proteins under a very wide
【机 构】
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Krebs Institute,The University of Sheffield,Sheffield S10 2TN and Manchester Institute of Biotechnol
【出 处】
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第九届IUPAC化学生物学国际研讨会暨第八届世界华人药物化学研讨会
论文部分内容阅读
Using a combination of multinuclear NMR spectroscopy,high resolution X-ray crystallography and computational chemistry we are able to examine the conformational behaviour of proteins under a very wide range of conditions.Recently,we have focussed on enzymes that catalyse the transfer of phosphoryl groups,where the non-catalysed reactions can be among the slowest known for a physiological process:phosphate monoesters,for example,have calculated lifetimes to spontaneous hydrolysis of up to 1012 years.I will use a range ofphosphoryl transfer enzymes to illustrate what contributes to the very high levels of catalysis achieved by these enzymes.Specifically,we have examined what happens during domain folding,during assembly of the native enzyme,during substrate binding,and during transition state binding.
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