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pubmed-article:21543228pubmed:issue11lld:pubmed
pubmed-article:21543228pubmed:dateCreated2011-5-25lld:pubmed
pubmed-article:21543228pubmed:abstractTextAn 11-mer peptide taken from a subsequence of the human protein ubiquitin was synthesized. The peptide has been fully characterized by NMR spectroscopy using chemical shift analysis and by NOE measurements. The conformation was calculated using state of the art MD methods of protein chemistry. A hairpin conformation was found which is to a large part identical with the structure of this peptide fragment within the human ubiquitin. The surprising result that already an 11-mer peptide adopts a hairpin conformation in aqueous solution is discussed in terms of initials sites for protein folding.lld:pubmed
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pubmed-article:21543228pubmed:authorpubmed-author:BergerStefanSlld:pubmed
pubmed-article:21543228pubmed:authorpubmed-author:SingerDavidDlld:pubmed
pubmed-article:21543228pubmed:authorpubmed-author:JahrNicoleNlld:pubmed
pubmed-article:21543228pubmed:authorpubmed-author:MeiChong...lld:pubmed
pubmed-article:21543228pubmed:copyrightInfoCopyright © 2011 Elsevier Ltd. All rights reserved.lld:pubmed
pubmed-article:21543228pubmed:issnTypeElectroniclld:pubmed
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pubmed-article:21543228pubmed:volume19lld:pubmed
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pubmed-article:21543228pubmed:year2011lld:pubmed
pubmed-article:21543228pubmed:articleTitleHairpin conformation of an 11-mer peptide.lld:pubmed
pubmed-article:21543228pubmed:affiliationInstitute of Analytical Chemistry, University Leipzig, Leipzig, Germany.lld:pubmed
pubmed-article:21543228pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:21543228pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed