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Titlebook: Chemical Recognition in Biology; F. Chapeville,A.-L. Haenni Book 1980 Springer-Verlag Berlin · Heidelberg 1980 Eiweisssynthese.Enzymatisch

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书目名称Chemical Recognition in Biology
编辑F. Chapeville,A.-L. Haenni
视频videohttp://file.papertrans.cn/225/224409/224409.mp4
丛书名称Molecular Biology, Biochemistry and Biophysics‘ Molekularbiologie, Biochemie und Biophysik
图书封面Titlebook: Chemical Recognition in Biology;  F. Chapeville,A.-L. Haenni Book 1980 Springer-Verlag Berlin · Heidelberg 1980 Eiweisssynthese.Enzymatisch
描述Studies of chemical recognition in biology were initiated about half a century ago with the flrst kinetic data obtained on enzyme catalysis and inhibition. They led to a rather static representation of the recognition process illustrated by the lock and key model that still continues to influence our overall image of recognition and its specificity. In several cases, crystallographic studies of enzyme-substrate complexes have supported this model. Indeed, in a crystallized ligand-enzyme complex, a close fltting is observed between the active center of the enzyme and the functional groups of the ligand. How­ ever, this does not necessarily result from a direct recognition process between rigid structures, but may result from a progressive adaptation during which the initial struc­ tures of the enzyme and the ligand are modified (induced-flt mechanism). Recently, a great deal of work has been devoted to the study of recognition in more complex systems such as the replication or the translation machin~ries; clearly, the extraordinary precision of such systems cannot be explained solely in terms of physical matching between enzymes and their substrates. This has led to a noticeable cha
出版日期Book 1980
关键词Eiweisssynthese; Enzymatische Regulation; adaptation; biology; enzymes; translation
版次1
doihttps://doi.org/10.1007/978-3-642-81503-4
isbn_softcover978-3-642-81505-8
isbn_ebook978-3-642-81503-4Series ISSN 0077-0221
issn_series 0077-0221
copyrightSpringer-Verlag Berlin · Heidelberg 1980
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Multi-Stage Efficiency Analysisrk in 1957. By then he had numerous scientific progeny, and my relationship to him is complicated by the fact that I can also count myself among his scientific grandchildren through apprenticeships with Hans Bomann and Bill Jencks. A good deal of what I am going to say, about enzyme interactions wit
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