Clays as possible catalysts for peptide formation in the prebiotic era.
Identifieur interne : 002B15 ( PubMed/Corpus ); précédent : 002B14; suivant : 002B16Clays as possible catalysts for peptide formation in the prebiotic era.
Auteurs : M. Paecht-HorowitzSource :
- Origins of life [ 0302-1688 ] ; 1976.
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- MESH :
Abstract
From the point of view of prebiotic synthesis, clays might have performed functions of concentration, catalysis, and protection of molecules. The degree of polymerization obtained when amino acid adenylates are added to montmorillonite suspensions in water, are much iigher than those obtained by polymerization in the absence of such a clay. In addition, they are of a discrete spectrum, usually multiplies of 6 or 7, and reach values of up to 40 mers. In the absence of clay a continuous spectrum of degrees of polymerization is obtained, and usually up to 4-6 mers only. Copolymerization in the absence of clays yields mostly random copolymers in their presence mostly block copolymers are obtained. Optical density measurements show that after adsorption has taken place on the clay, stacking of its layers occurs. Polymerization starts only after these stacked layers have been formed. The distance between the layers - as measured by X-rays - increase during polymerization, probably because the resulting polymers settle in their interspace, while the adsorption site of the active monomers is at the edges of the clay.
DOI: 10.1007/bf00927932
PubMed: 1023136
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pubmed:1023136Le document en format XML
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Paecht-Horowitz</name></author></analytic><series><title level="j">Origins of life</title><idno type="ISSN">0302-1688</idno><imprint><date when="1976" type="published">1976</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Monophosphate</term><term>Catalysis</term><term>Peptides</term><term>Soil</term><term>Spectrum Analysis</term><term>Structure-Activity Relationship</term><term>Water</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adenosine Monophosphate</term><term>Peptides</term><term>Soil</term><term>Water</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Spectrum Analysis</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">From the point of view of prebiotic synthesis, clays might have performed functions of concentration, catalysis, and protection of molecules. The degree of polymerization obtained when amino acid adenylates are added to montmorillonite suspensions in water, are much iigher than those obtained by polymerization in the absence of such a clay. In addition, they are of a discrete spectrum, usually multiplies of 6 or 7, and reach values of up to 40 mers. In the absence of clay a continuous spectrum of degrees of polymerization is obtained, and usually up to 4-6 mers only. Copolymerization in the absence of clays yields mostly random copolymers in their presence mostly block copolymers are obtained. Optical density measurements show that after adsorption has taken place on the clay, stacking of its layers occurs. Polymerization starts only after these stacked layers have been formed. The distance between the layers - as measured by X-rays - increase during polymerization, probably because the resulting polymers settle in their interspace, while the adsorption site of the active monomers is at the edges of the clay.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1023136</PMID><DateCompleted><Year>1977</Year><Month>05</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0302-1688</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>4</Issue><PubDate><Year>1976</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Origins of life</Title><ISOAbbreviation>Orig. Life</ISOAbbreviation></Journal><ArticleTitle>Clays as possible catalysts for peptide formation in the prebiotic era.</ArticleTitle><Pagination><MedlinePgn>369-81</MedlinePgn></Pagination><Abstract><AbstractText>From the point of view of prebiotic synthesis, clays might have performed functions of concentration, catalysis, and protection of molecules. The degree of polymerization obtained when amino acid adenylates are added to montmorillonite suspensions in water, are much iigher than those obtained by polymerization in the absence of such a clay. In addition, they are of a discrete spectrum, usually multiplies of 6 or 7, and reach values of up to 40 mers. In the absence of clay a continuous spectrum of degrees of polymerization is obtained, and usually up to 4-6 mers only. Copolymerization in the absence of clays yields mostly random copolymers in their presence mostly block copolymers are obtained. Optical density measurements show that after adsorption has taken place on the clay, stacking of its layers occurs. Polymerization starts only after these stacked layers have been formed. The distance between the layers - as measured by X-rays - increase during polymerization, probably because the resulting polymers settle in their interspace, while the adsorption site of the active monomers is at the edges of the clay.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Paecht-Horowitz</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Orig Life</MedlineTA><NlmUniqueID>0420542</NlmUniqueID><ISSNLinking>0302-1688</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012987">Soil</NameOfSubstance></Chemical><Chemical><RegistryNumber>059QF0KO0R</RegistryNumber><NameOfSubstance UI="D014867">Water</NameOfSubstance></Chemical><Chemical><RegistryNumber>415SHH325A</RegistryNumber><NameOfSubstance UI="D000249">Adenosine Monophosphate</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>S</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000249" MajorTopicYN="N">Adenosine Monophosphate</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="Y">Peptides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012987" MajorTopicYN="Y">Soil</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013057" MajorTopicYN="N">Spectrum Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014867" MajorTopicYN="N">Water</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NASA">77147863</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1976</Year><Month>12</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1976</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1976</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1023136</ArticleId><ArticleId IdType="doi">10.1007/bf00927932</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nature. 1970 Nov 14;228(5272):636-9</Citation><ArticleIdList><ArticleId IdType="pubmed">5474935</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1967 Dec 14;30(2):223-53</Citation><ArticleIdList><ArticleId IdType="pubmed">4297187</ArticleId></ArticleIdList></Reference><Reference><Citation>Orig Life. 1974 Jan-Apr;5(1):173-87</Citation><ArticleIdList><ArticleId IdType="pubmed">4842069</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1971 Oct 1;174(4004):53-5</Citation><ArticleIdList><ArticleId IdType="pubmed">17755695</ArticleId></ArticleIdList></Reference><Reference><Citation>Angew Chem Int Ed Engl. 1973 May;12(5):349-56</Citation><ArticleIdList><ArticleId IdType="pubmed">4200276</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1964 Aug 19;90:260-81</Citation><ArticleIdList><ArticleId IdType="pubmed">14220711</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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