title: Hairpin conformation of an 11-mer peptide.
abstract: An 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.
authors.affiliation: Institute of Analytical Chemistry, University Leipzig, Leipzig, Germany.
authors.forename: Chong Geok
authors.initials: CG
authors.lastname: Mei
authors.forename: Nicole
authors.initials: N
authors.lastname: Jahr
authors.forename: David
authors.initials: D
authors.lastname: Singer
authors.forename: Stefan
authors.initials: S
authors.lastname: Berger
mesh_terms: D006801:Humans; D055029:Inverted Repeat Sequences; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D010455:Peptides; D025801:Ubiquitin