Journal of Biomolecular Structure and Dynamics · 1990 · 11 citations · 28 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryStructural BiochemistryStructural BiologyMacromolecular StructurePeptide ChemistryProtein ConformationProtein StructureSecondary StructureTertiary StructureAlpha HelicesAlpha-helix FormationBeta-turn FormationHydrophobic InteractionsMolecular Conformation In SolutionPeptide Structure AnalysisProtein Secondary Structure AnalysisTriple Helix Structure
The high-field 1H and 13C NMR studies of the N- and C-terminal telopeptides of the alpha-2 chain of collagen were carried out in CD3OH/H2O solutions. All proton assignments are based on two-dimensional phase-sensitive COSY and ROESY experiments. The conformation of the N-telopeptide (nonamer) is predominantly extended with a small proportion of the molecules existing in a type I beta turn. The four residues involved in this turn are D3-A4-K5-G6 which is stabilized by a C = O(D3)-NH(G6) hydrogen bond. The C-terminal telopeptide is extended throughout. A model is proposed involving charge-charge and hydrophobic interactions between the extended alpha-2 chain N-telopeptide and the adjacent segments of triple-helix. A similar model is proposed for the C-telopeptide.
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