| The mechanism of clay catalyzed polymerization of amino acid adenylates. | |
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MedLine Citation:
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PMID: 20183 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Amino acid adenylates were adsorbed on montmorillonite when either the interspatial faces or the edges of the latter were blocked. By this method it could be observed that adsorption of the amino acid adenylates takes place mostly on the planes of the clay. However, for polymerization to take place, the edges of the clay have to be free as well and apparently only these molecules polymerize which are attached to the planes of the clay by their amino groups and to the edges of the clay by their phosphate group. Thus all the charges of the molecules which might produce their repulsion from each other would be neutralized. As a consequence of these attachments polymerization on the clay would take place on its planar sites, but only on those neighboring its edges. The question whether neutralization of charges is also the reason why biochemical substrates have to attach themselves by several points to enzymes and thus make biochemistry fit into the framework of general chemistry, is raised. |
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Authors:
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M Paecht-Horowitz |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Bio Systems Volume: 9 ISSN: 0303-2647 ISO Abbreviation: BioSystems Publication Date: 1977 Sep |
Date Detail:
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Created Date: 1977-11-30 Completed Date: 1977-11-30 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0430773 Medline TA: Biosystems Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 93-8 Citation Subset: IM; S |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Monophosphate
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analogs & derivatives* Adsorption Alanine / analogs & derivatives* Biogenesis* Catalysis Hydrogen-Ion Concentration Minerals* Peptides / chemical synthesis* Structure-Activity Relationship |
| Chemical | |
Reg. No./Substance:
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0/Minerals; 0/Peptides; 56-41-7/Alanine; 61-19-8/Adenosine Monophosphate |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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