1s1o
From Proteopedia
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NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix
Overview
Conformational characteristics of alternating D,L linear peptides are of, particular interest because of their capacity to form transmembrane, channels with different transport properties, as some natural antibiotics, do. Single- and double-stranded beta-helical structures are common for, alternating D,L peptides. The stability of the beta-helix depends on, several structural factors, such as the backbone peptide length, type and, position of side chains, and nature of terminal groups. The NMR and, molecular dynamics solution conformation of a synthetic alternating, D,L-oligopeptide with 15 norleucines (XVMe) has been used as a model to, get insight in to the conformational features of double-stranded, beta-helix structures. The NH chemical shift values (delta(NH)) and, long-range nuclear Overhauser effects (NOE) cross peaks, in particular, interstrand connectivities, clearly point to an antiparallel, double-stranded beta-helix for the XVMe major conformation in solution. An, extensive set of distances (from NOE cross peaks) and H-bonds (from, delta(NH)) has been included in the molecular dynamics calculations. The, experimental NMR data and theoretical calculations clearly indicate that, the most probable conformation of XVMe in solution is a double-strand, antiparallel beta(5.6) increasing decreasing-helix structure.
About this Structure
1S1O is a Protein complex structure of sequences from [1] with BOC as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of a D,L-alternating oligonorleucine as a model of double-stranded antiparallel beta-helix., Navarro E, Fenude E, Celda B, Biopolymers. 2002 Aug 5;64(4):198-209. PMID:12115137
Page seeded by OCA on Sat Nov 24 23:42:21 2007
Categories: Protein complex | Celda, B. | Fennude, E. | Navarro, E. | BOC | Beta-helix | D | Gramicidin | L-alternating | Norleucine
