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Article: A Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimer

TitleA Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimer
Authors
Issue Date2003
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, 2003, v. 125 n. 47, p. 14452-14457 How to Cite?
AbstractOur previous work revealed that two adjacent D-α-aminoxy acids could form two homochiral N-O turns, with the backbone folding into an extended helical structure (1.8 8-helix). Here, we report the conformational studies of linear peptides 3-6, which contain a D,L-α-aminoxy acid dimer segment. The NMR and X-ray analysis of 3 showed that it folded into a loop conformation with two heterochiral N-O turns. This loop segment can be used to constrain tetrapeptides 4 and 6 to form a reverse turn structure. 1H NMR dilution studies, DMSO-d 6 addition studies, and 2D-NOESY data indicated that tetrapeptides 4 and 6 folded into reverse turn conformations featured by a head-to-tail 16-membered-ring intramolecular hydrogen bond. In contrast, tetrapeptide 5 with L-Ala instead of Gly or D-Ala as the N-terminal amino acid could not form the desired reverse turn structure for steric reasons. Quantum mechanics calculations showed that model pentamide 7, with the same substitution pattern of 4, adopted a novel reverse turn conformation featuring two heterochiral N-O turns (each of an 8-membered ring hydrogen bond), a cross-strand 16-membered ring hydrogen bond, and a 7-membered ring γ-turn.
Persistent Identifierhttp://hdl.handle.net/10722/167852
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYang, Den_US
dc.contributor.authorQu, Jen_US
dc.contributor.authorLi, Wen_US
dc.contributor.authorWang, DPen_US
dc.contributor.authorRen, Yen_US
dc.contributor.authorWu, YDen_US
dc.date.accessioned2012-10-08T03:12:13Z-
dc.date.available2012-10-08T03:12:13Z-
dc.date.issued2003en_US
dc.identifier.citationJournal Of The American Chemical Society, 2003, v. 125 n. 47, p. 14452-14457en_US
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://hdl.handle.net/10722/167852-
dc.description.abstractOur previous work revealed that two adjacent D-α-aminoxy acids could form two homochiral N-O turns, with the backbone folding into an extended helical structure (1.8 8-helix). Here, we report the conformational studies of linear peptides 3-6, which contain a D,L-α-aminoxy acid dimer segment. The NMR and X-ray analysis of 3 showed that it folded into a loop conformation with two heterochiral N-O turns. This loop segment can be used to constrain tetrapeptides 4 and 6 to form a reverse turn structure. 1H NMR dilution studies, DMSO-d 6 addition studies, and 2D-NOESY data indicated that tetrapeptides 4 and 6 folded into reverse turn conformations featured by a head-to-tail 16-membered-ring intramolecular hydrogen bond. In contrast, tetrapeptide 5 with L-Ala instead of Gly or D-Ala as the N-terminal amino acid could not form the desired reverse turn structure for steric reasons. Quantum mechanics calculations showed that model pentamide 7, with the same substitution pattern of 4, adopted a novel reverse turn conformation featuring two heterochiral N-O turns (each of an 8-membered ring hydrogen bond), a cross-strand 16-membered ring hydrogen bond, and a 7-membered ring γ-turn.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_US
dc.relation.ispartofJournal of the American Chemical Societyen_US
dc.subject.meshAmino Acids - Chemistryen_US
dc.subject.meshDimerizationen_US
dc.subject.meshHydrogen Bondingen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshOligopeptides - Chemistryen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.titleA Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimeren_US
dc.typeArticleen_US
dc.identifier.emailYang, D:yangdan@hku.hken_US
dc.identifier.authorityYang, D=rp00825en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja029514jen_US
dc.identifier.pmid14624594-
dc.identifier.scopuseid_2-s2.0-0345306283en_US
dc.identifier.hkuros91770-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0345306283&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume125en_US
dc.identifier.issue47en_US
dc.identifier.spage14452en_US
dc.identifier.epage14457en_US
dc.identifier.isiWOS:000186722200061-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYang, D=7404800756en_US
dc.identifier.scopusauthoridQu, J=7201534485en_US
dc.identifier.scopusauthoridLi, W=36066858500en_US
dc.identifier.scopusauthoridWang, DP=7407069947en_US
dc.identifier.scopusauthoridRen, Y=7403274496en_US
dc.identifier.scopusauthoridWu, YD=7406892738en_US
dc.identifier.citeulike3425287-

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