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Deuterium Exchange in Polypeptides
OBSERVATIONS on the rate of deuteration of the NH groups in solutions of proteins in heavy water (see, for example, ref. 1) have shown that in some proteins there is both a fast and a slow exchange, and it has been conjectured that those NH groups which exchange slowly are hydrogen-bonded in α-helix...
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Published in: | Nature (London) 1958-09, Vol.182 (4636), p.654-655 |
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description | OBSERVATIONS on the rate of deuteration of the NH groups in solutions of proteins in heavy water (see, for example, ref. 1) have shown that in some proteins there is both a fast and a slow exchange, and it has been conjectured that those NH groups which exchange slowly are hydrogen-bonded in α-helix arrangements, whereas the fast reaction is associated with solvated NH groups. This possibility can be more profitably examined in solutions of a simple polypeptide such as poly-γ-benzyl-
L
-glutamate, where the conditions for α-helical or random, solvated coil forms are now well-known
2,3
. Doty and Yang
3
have shown that in mixtures of dichloracetic acid and ethylene dichloride, samples of poly-γ-benzyl-
L
-glutamate of high molecular weight may exist either in α-helix or in random coil forms, according to the composition of the solvent. |
doi_str_mv | 10.1038/182654b0 |
format | article |
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L
-glutamate, where the conditions for α-helical or random, solvated coil forms are now well-known
2,3
. Doty and Yang
3
have shown that in mixtures of dichloracetic acid and ethylene dichloride, samples of poly-γ-benzyl-
L
-glutamate of high molecular weight may exist either in α-helix or in random coil forms, according to the composition of the solvent.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/182654b0</identifier><identifier>PMID: 13590054</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Deuterium ; Humanities and Social Sciences ; letter ; multidisciplinary ; Old Medline ; Peptides - metabolism ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 1958-09, Vol.182 (4636), p.654-655</ispartof><rights>Springer Nature Limited 1958</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c336t-4fed04f6c0608991ddf443a87c85c2c9815be5ad7535970ab2bb3e4b496494f63</citedby><cites>FETCH-LOGICAL-c336t-4fed04f6c0608991ddf443a87c85c2c9815be5ad7535970ab2bb3e4b496494f63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13590054$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ELLIOTT, A</creatorcontrib><creatorcontrib>HANBY, W. E</creatorcontrib><title>Deuterium Exchange in Polypeptides</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>OBSERVATIONS on the rate of deuteration of the NH groups in solutions of proteins in heavy water (see, for example, ref. 1) have shown that in some proteins there is both a fast and a slow exchange, and it has been conjectured that those NH groups which exchange slowly are hydrogen-bonded in α-helix arrangements, whereas the fast reaction is associated with solvated NH groups. This possibility can be more profitably examined in solutions of a simple polypeptide such as poly-γ-benzyl-
L
-glutamate, where the conditions for α-helical or random, solvated coil forms are now well-known
2,3
. Doty and Yang
3
have shown that in mixtures of dichloracetic acid and ethylene dichloride, samples of poly-γ-benzyl-
L
-glutamate of high molecular weight may exist either in α-helix or in random coil forms, according to the composition of the solvent.</description><subject>Deuterium</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>multidisciplinary</subject><subject>Old Medline</subject><subject>Peptides - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1958</creationdate><recordtype>article</recordtype><recordid>eNp9kE1Lw0AQhhdRbK2Cv0CKB9FDdDb7kc1Rav2Agh70vGw2E03Jl7sJ2H_vSlp68zQM88wzzEvIOYVbCkzdURVLwTM4IFPKExlxqZJDMgWIVQSKyQk58X4NAIIm_JhMKBNpaPiUXD7g0KMrh3q-_LFfpvnEednM39pq02HXlzn6U3JUmMrj2bbOyMfj8n3xHK1en14W96vIMib7iBeYAy-kBQkqTWmeF5wzoxKrhI1tqqjIUJg8EeF4AiaLs4whz3gqeRr22Ixcjd7Otd8D-l7XpbdYVabBdvBaxXGsgPEAXo-gda33DgvdubI2bqMp6L889C6PgF5snUNWY74HtwEE4GYEfBiF551et4Nrwp__yBrTDw73sh3wCz_Cb68</recordid><startdate>19580906</startdate><enddate>19580906</enddate><creator>ELLIOTT, A</creator><creator>HANBY, W. E</creator><general>Nature Publishing Group UK</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19580906</creationdate><title>Deuterium Exchange in Polypeptides</title><author>ELLIOTT, A ; HANBY, W. E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c336t-4fed04f6c0608991ddf443a87c85c2c9815be5ad7535970ab2bb3e4b496494f63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1958</creationdate><topic>Deuterium</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>multidisciplinary</topic><topic>Old Medline</topic><topic>Peptides - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ELLIOTT, A</creatorcontrib><creatorcontrib>HANBY, W. E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ELLIOTT, A</au><au>HANBY, W. E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Deuterium Exchange in Polypeptides</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1958-09-06</date><risdate>1958</risdate><volume>182</volume><issue>4636</issue><spage>654</spage><epage>655</epage><pages>654-655</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>OBSERVATIONS on the rate of deuteration of the NH groups in solutions of proteins in heavy water (see, for example, ref. 1) have shown that in some proteins there is both a fast and a slow exchange, and it has been conjectured that those NH groups which exchange slowly are hydrogen-bonded in α-helix arrangements, whereas the fast reaction is associated with solvated NH groups. This possibility can be more profitably examined in solutions of a simple polypeptide such as poly-γ-benzyl-
L
-glutamate, where the conditions for α-helical or random, solvated coil forms are now well-known
2,3
. Doty and Yang
3
have shown that in mixtures of dichloracetic acid and ethylene dichloride, samples of poly-γ-benzyl-
L
-glutamate of high molecular weight may exist either in α-helix or in random coil forms, according to the composition of the solvent.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>13590054</pmid><doi>10.1038/182654b0</doi><tpages>2</tpages></addata></record> |
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subjects | Deuterium Humanities and Social Sciences letter multidisciplinary Old Medline Peptides - metabolism Science Science (multidisciplinary) |
title | Deuterium Exchange in Polypeptides |
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