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Titlebook: Enzyme Physics; Mikhail V. Vol’kenshtein Book 1969 Springer Science+Business Media New York 1969 enzymes.kinetics.molecule.proteins

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发表于 2025-3-21 18:11:22 | 显示全部楼层 |阅读模式
书目名称Enzyme Physics
编辑Mikhail V. Vol’kenshtein
视频videohttp://file.papertrans.cn/314/313092/313092.mp4
图书封面Titlebook: Enzyme Physics;  Mikhail V. Vol’kenshtein Book 1969 Springer Science+Business Media New York 1969 enzymes.kinetics.molecule.proteins
描述This book treats a new, far-from-fully-developed area of molecular biophysics-enzyme physics. An attempt is made to survey this field, but primary consideration is given tothreeprob­ lems under investigation in the Polymer Structure Labaratory of the Institue of High-Molecular Compounds, Academy of Seiences ofthe USSR. The first problern is the genetic coding of the biologically fun.ctional structure of proteins. Its solution is based on physical theories of hydrophobic interactions. The second problern is the conformational properties of pro­ teins as the factor governing enzyme activity. The most direct methods for experimental investigation of questions in this area are optical, principally those involving natural and magnetic rota­ tion of the plane of polarization. A substantial portion of the book concerns optical activity; the Faraday effect is discussed in an appendix. The third problern is the manifestation of the cooperative properties of enzymes in the kinetics of enzymatic reactions and the solution of complex kinetic problems. This problern is espe­ cially pressing in connection with research on allosteric enzymes, which are responsible for feedback in metabolic proces
出版日期Book 1969
关键词enzymes; kinetics; molecule; proteins
版次1
doihttps://doi.org/10.1007/978-1-4899-2834-4
isbn_softcover978-1-4899-2836-8
isbn_ebook978-1-4899-2834-4
copyrightSpringer Science+Business Media New York 1969
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发表于 2025-3-21 21:44:09 | 显示全部楼层
Hydrophobic Interactions and Protein Structure,ilize the globule. The formation of ionic aggregates, which is considered by Saroff [24], cannot be regarded as the principal factor responsible for such stabilization and is not sufficient to account for it. Generally speaking, one cannot draw-any serious conclusions regarding the three-dimensional
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Macromolecular Properties of Enzymes,and physicochemical properties of the amino acid residues, which interact with the compounds participating in the reaction catalyzed. Braunshtein quite clearly indicated the factors that operate in enzymatic catalysis [53, 53a]:
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Optical Activity of Polypeptide Chains,rotein is synthesized on template RNA through the intermediary of tRNA molecules. The asymmetry of RNA is caused by that of the carbohydrate groups of ribose. It is precisely this factor that makes .- and .-amino acids nonequivalent with respect to incorporation into polypeptide chains. Proteins are
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Conformational Properties of Enzymes and Ionization,rates, inhibitors, and activators, i.e., in any effector. Enzymatic activity thus depends to a large extent on medium pH and hence on the degree of ionization of the corresponding groups. Inhibition and activation of an enzyme also depend on pH. The aforementioned bell-shaped curve dependence on pH
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Cooperative Properties of Enzymes and Reaction Kinetics,rative in character, so that the development of induced structural correspondence between an enzyme and substrate is itself a cooperative process. In this sense, enzymatic activity is based on the same phenomena that produce the elasticity of rubber, i.e., those of cooperative rotational isomer-izat
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Allosteric Enzymes, whole are highly advanced self-regulating systems. The occurrence of regulation implies the existence of communications pathways along which appropriate information is transmitted. Moreover, self-regulation requires feedback; the control apparatus must receive information on the state of the system
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