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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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發(fā)表于 2025-3-23 12:36:19 | 只看該作者
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發(fā)表于 2025-3-23 14:36:33 | 只看該作者
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發(fā)表于 2025-3-23 21:55:23 | 只看該作者
Nimrod and Dead Prez: Walking Like a Warrior ribose. It is precisely this factor that makes .- and .-amino acids nonequivalent with respect to incorporation into polypeptide chains. Proteins are built up from .-amino acids [3]. We should be grateful to nature for this, since optical activity gives us valuable opportunities for studying their structure.
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發(fā)表于 2025-3-24 00:27:47 | 只看該作者
William A. Darity Jr.,Patrick L. Masonthis sense, enzymatic activity is based on the same phenomena that produce the elasticity of rubber, i.e., those of cooperative rotational isomer-ization [2, 206], An understanding of this important hypothesis is the starting point for enzyme physics, whose development has only just begun.
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發(fā)表于 2025-3-24 05:03:53 | 只看該作者
Hydrophobic Interactions and Protein Structure, structure of a protein without taking into account the actual conditions under which its native structure exists in the aqueous medium. A biologically functional protein exists in water and not in isolation. Water is a liquid having very special properties and the aqueous environment has a decisive effect on protein structure.
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Book 1969sideration 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
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發(fā)表于 2025-3-24 20:02:03 | 只看該作者
20#
發(fā)表于 2025-3-25 00:08:22 | 只看該作者
Cooperative Properties of Enzymes and Reaction Kinetics,this sense, enzymatic activity is based on the same phenomena that produce the elasticity of rubber, i.e., those of cooperative rotational isomer-ization [2, 206], An understanding of this important hypothesis is the starting point for enzyme physics, whose development has only just begun.
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