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pubmed-article:11429814rdf:typepubmed:Citationlld:pubmed
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pubmed-article:11429814pubmed:dateCreated2001-6-29lld:pubmed
pubmed-article:11429814pubmed:abstractTextThis paper describes conformational studies of proline-templated amino acids (PTAAs) based on the 3-azabicyclo[3.1.0]hexane system as well as conformational studies on short peptides composed of these PTAAs. NOE data, coupling constants, and molecular modeling are consistent with a flattened boat conformation for monomeric and oligomeric residues based on this bicyclic system. NMR studies on dimeric and trimeric oligomers are consistent with a populated poly-L-proline type II conformation in CDCl3 and D2O. Solution studies and molecular modeling predicts phi approximately -70 degrees, psi approximately 131 degrees, chi 1 approximately -57 degrees, and chi 2 approximately -158 degrees for oligomeric residues.lld:pubmed
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pubmed-article:11429814pubmed:issn0022-3263lld:pubmed
pubmed-article:11429814pubmed:authorpubmed-author:ZhangRRlld:pubmed
pubmed-article:11429814pubmed:authorpubmed-author:NatarajanAAlld:pubmed
pubmed-article:11429814pubmed:authorpubmed-author:Madalengoitia...lld:pubmed
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pubmed-article:11429814pubmed:volume66lld:pubmed
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pubmed-article:11429814pubmed:pagination455-60lld:pubmed
pubmed-article:11429814pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11429814pubmed:year2001lld:pubmed
pubmed-article:11429814pubmed:articleTitlePoly-L-proline type II peptide mimics based on the 3-azabicyclo[3.1.0]hexane system.lld:pubmed
pubmed-article:11429814pubmed:affiliationDepartment of Chemistry, University of Vermont, Burlington, Vermont 05405, USA.lld:pubmed
pubmed-article:11429814pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11429814pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:11429814pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed