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- Publisher Website: 10.1021/ja029514j
- Scopus: eid_2-s2.0-0345306283
- PMID: 14624594
- WOS: WOS:000186722200061
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Article: A Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimer
Title | A Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimer |
---|---|
Authors | |
Issue Date | 2003 |
Publisher | American 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? |
Abstract | Our 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 Identifier | http://hdl.handle.net/10722/167852 |
ISSN | 2023 Impact Factor: 14.4 2023 SCImago Journal Rankings: 5.489 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yang, D | en_US |
dc.contributor.author | Qu, J | en_US |
dc.contributor.author | Li, W | en_US |
dc.contributor.author | Wang, DP | en_US |
dc.contributor.author | Ren, Y | en_US |
dc.contributor.author | Wu, YD | en_US |
dc.date.accessioned | 2012-10-08T03:12:13Z | - |
dc.date.available | 2012-10-08T03:12:13Z | - |
dc.date.issued | 2003 | en_US |
dc.identifier.citation | Journal Of The American Chemical Society, 2003, v. 125 n. 47, p. 14452-14457 | en_US |
dc.identifier.issn | 0002-7863 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167852 | - |
dc.description.abstract | Our 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.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html | en_US |
dc.relation.ispartof | Journal of the American Chemical Society | en_US |
dc.subject.mesh | Amino Acids - Chemistry | en_US |
dc.subject.mesh | Dimerization | en_US |
dc.subject.mesh | Hydrogen Bonding | en_US |
dc.subject.mesh | Models, Molecular | en_US |
dc.subject.mesh | Nuclear Magnetic Resonance, Biomolecular | en_US |
dc.subject.mesh | Oligopeptides - Chemistry | en_US |
dc.subject.mesh | Protein Conformation | en_US |
dc.subject.mesh | Protein Structure, Secondary | en_US |
dc.title | A Reverse Turn Structure Induced by a D,L-α-Aminoxy Acid Dimer | en_US |
dc.type | Article | en_US |
dc.identifier.email | Yang, D:yangdan@hku.hk | en_US |
dc.identifier.authority | Yang, D=rp00825 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1021/ja029514j | en_US |
dc.identifier.pmid | 14624594 | - |
dc.identifier.scopus | eid_2-s2.0-0345306283 | en_US |
dc.identifier.hkuros | 91770 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0345306283&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 125 | en_US |
dc.identifier.issue | 47 | en_US |
dc.identifier.spage | 14452 | en_US |
dc.identifier.epage | 14457 | en_US |
dc.identifier.isi | WOS:000186722200061 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Yang, D=7404800756 | en_US |
dc.identifier.scopusauthorid | Qu, J=7201534485 | en_US |
dc.identifier.scopusauthorid | Li, W=36066858500 | en_US |
dc.identifier.scopusauthorid | Wang, DP=7407069947 | en_US |
dc.identifier.scopusauthorid | Ren, Y=7403274496 | en_US |
dc.identifier.scopusauthorid | Wu, YD=7406892738 | en_US |
dc.identifier.citeulike | 3425287 | - |
dc.identifier.issnl | 0002-7863 | - |