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Article: γ4-Aminoxy peptides as new peptidomimetic foldamers

Titleγ4-Aminoxy peptides as new peptidomimetic foldamers
Authors
Chen, FZhu, NYYang, D
Issue Date2004
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2004, v. 126 n. 49, p. 15980-15981 How to Cite?
DOI: http://dx.doi.org/10.1021/ja044493+
AbstractThe conformational properties of peptides 1-3 of γ-aminoxy acids have been investigated by using FT-IR, NMR spectroscopy, and X-ray crystallography. Diamide 1 consisting of unsubstituted γ-aminoxy acid cannot form intramolecular hydrogen bond. A novel γ N-O turn involving a 10-membered-ring intramolecular hydrogen bond between NH i+2 and CO i is formed in γ 4-aminoxy peptides 2 and 3. Triamides 3 prefers a new helical structure featuring two consecutive γ N-O turns. Therefore, γ 4-aminoxy peptides represent new peptidomimetic foldamers. Copyright © 2004 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/167877
ISSN
0002-7863
2023 Impact Factor: 14.4
2023 SCImago Journal Rankings: 5.489
ISI Accession Number ID
WOS:000225697000028
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorChen, Fen_HK
dc.contributor.authorZhu, NYen_HK
dc.contributor.authorYang, Den_HK
dc.date.accessioned2012-10-08T03:12:26Z-
dc.date.available2012-10-08T03:12:26Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2004, v. 126 n. 49, p. 15980-15981en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/167877-
dc.description.abstractThe conformational properties of peptides 1-3 of γ-aminoxy acids have been investigated by using FT-IR, NMR spectroscopy, and X-ray crystallography. Diamide 1 consisting of unsubstituted γ-aminoxy acid cannot form intramolecular hydrogen bond. A novel γ N-O turn involving a 10-membered-ring intramolecular hydrogen bond between NH i+2 and CO i is formed in γ 4-aminoxy peptides 2 and 3. Triamides 3 prefers a new helical structure featuring two consecutive γ N-O turns. Therefore, γ 4-aminoxy peptides represent new peptidomimetic foldamers. Copyright © 2004 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.subject.meshAmino Acids - Chemistryen_US
dc.subject.meshBiomimetic Materials - Chemistryen_US
dc.subject.meshCircular Dichroismen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshPeptides - Chemistryen_US
dc.subject.meshProtein Foldingen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshSpectroscopy, Fourier Transform Infrareden_US
dc.titleγ4-Aminoxy peptides as new peptidomimetic foldamersen_HK
dc.typeArticleen_HK
dc.identifier.emailZhu, NY: nzhu@hkucc.hku.hken_HK
dc.identifier.emailYang, D: yangdan@hku.hken_HK
dc.identifier.authorityZhu, NY=rp00845en_HK
dc.identifier.authorityYang, D=rp00825en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja044493+en_HK
dc.identifier.pmid15584729-
dc.identifier.scopuseid_2-s2.0-10344219514en_HK
dc.identifier.hkuros98424-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-10344219514&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume126en_HK
dc.identifier.issue49en_HK
dc.identifier.spage15980en_HK
dc.identifier.epage15981en_HK
dc.identifier.isiWOS:000225697000028-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChen, F=14070141300en_HK
dc.identifier.scopusauthoridZhu, NY=7201449530en_HK
dc.identifier.scopusauthoridYang, D=7404800756en_HK
dc.identifier.issnl0002-7863-

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