Statements in which the resource exists.
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pubmed-article:11563031rdf:typepubmed:Citationlld:pubmed
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pubmed-article:11563031pubmed:issue4-7lld:pubmed
pubmed-article:11563031pubmed:dateCreated2001-9-20lld:pubmed
pubmed-article:11563031pubmed:abstractTextThe influence of amino acid side chains [derived from: Ala, Val, Leu, Ile, Phe, Tyr(Bzl), Ser(Bzl), Thr(Bzl), Pro, Trp], incorporated into "aminoalkyl" part of PNA monomers, on the temperature-dependent distributions of rotamers about the tertiary amide bond was studied by means of 1H NMR at 0, 25 and 40 degrees C in CDCl3. The delta G0 values of the energy differences between individual rotamers were calculated. The results may be helpful in the designing of monomers with desirable properties.lld:pubmed
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pubmed-article:11563031pubmed:statusMEDLINElld:pubmed
pubmed-article:11563031pubmed:issn1525-7770lld:pubmed
pubmed-article:11563031pubmed:authorpubmed-author:OleszczukMMlld:pubmed
pubmed-article:11563031pubmed:authorpubmed-author:FalkiewiczBBlld:pubmed
pubmed-article:11563031pubmed:authorpubmed-author:Rodziewicz-Mo...lld:pubmed
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pubmed-article:11563031pubmed:volume20lld:pubmed
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pubmed-article:11563031pubmed:pagination1399-402lld:pubmed
pubmed-article:11563031pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11563031pubmed:articleTitleRestricted rotation in chiral peptide nucleic acid (PNA) monomers--influence of substituents studied by means of 1H NMR.lld:pubmed
pubmed-article:11563031pubmed:affiliationInstitute of Biochemistry and Biophysics, Polish Academy of Science, Warszawa, Poland.lld:pubmed
pubmed-article:11563031pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11563031pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed