Enzyme Physics by Mikhail V. Vol’kenshtein (auth.)

By Mikhail V. Vol’kenshtein (auth.)

This publication treats a brand new, far-from-fully-developed quarter of molecular biophysics-enzyme physics. An try out is made to survey this box, yet fundamental attention is given tothreeprob­ lems less than research within the Polymer constitution Labaratory of the Institue of High-Molecular Compounds, Academy of Seiences ofthe USSR. the 1st problern is the genetic coding of the biologically fun.ctional constitution of proteins. Its answer relies on actual theories of hydrophobic interactions. the second one problern is the conformational homes of professional­ teins because the issue governing enzyme job. the main direct equipment for experimental research of questions during this quarter are optical, mostly these concerning traditional and magnetic rota­ tion of the aircraft of polarization. a considerable section of the ebook matters optical job; the Faraday influence is mentioned in an appendix. The 3rd problern is the manifestation of the cooperative homes of enzymes within the kinetics of enzymatic reactions and the answer of complicated kinetic difficulties. This problern is espe­ cially urgent in reference to examine on allosteric enzymes, that are accountable for suggestions in metabolic methods. An appendix describes a brand new approach for fixing kinetic difficulties, in keeping with the idea of graphs. This quantity extends and information yes of the information ex­ pressed in my earlier booklet, Molecules and existence: An creation to Molecular Biophysics, which used to be released during this sequence in 1965.

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Example text

Nevertheless, there are some grounds for considering the Vibrations of the drop model to be responsible for the specific globule interaction in enzymes having a quaternary structure (see p. 116). Shnol' reported observing synchronaus fluctuations in the enzymatic activity of actin, myosili, and actomyosin in solution [69]. He suggested that the protein conformation varies, a process accompanied by a change in the hydrophilic-hydrophobic properties of the globule surface, which causes rearrangement of the water structure.

It is obvious that, if such selection of conformations actually occurs, it results from the real forces of the enzyme-substrate interaction. These forces increase with the number of atomic groups in the substrate that are in contact with functional groups of the protein. The interactions themselves are very diverse, because of the wide range of amino acid residues: they include chemical donor-acceptor and ionic bonds, electrostatic ion-dipole and dipole-dipole forces, hydrogen bonds, and hydrophobic interactions of nonpolar groups in an aqueous medium.

Carboxypeptidase B (hog) Carboxypeptidase • , • , . ••. ß -Lactoglobulin (bovine) Ovalbumin (chicken) ••• a-Amylase (B. • Leueine aminopeptidase . Phycocyanin (P. tenera) . Heavy meromyosin (rabbit1 a-Lipovitellin (egg yolk) Mol. wt. UCTURE Fig. 8, Three-dimensional protein structure (after Guzzo), The black dots represent hydrophobic groups, the circles represent hydrophilic groups, the cylinders represent cxhelices, and the spheres represent residues which do not form helices. 27 the molecular weight) rises.

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