 |
PDBsum entry 1s1o
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
De novo protein
|
PDB id
|
|
|
|
1s1o
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure of a d,L-Alternating oligonorleucine as a model of double-Stranded antiparallel beta-Helix.
|
|
|
Authors
|
|
E.Navarro,
E.Fenude,
B.Celda.
|
|
|
Ref.
|
|
Biopolymers, 2002,
64,
198-209.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
|
Headers
|
|
|
|
|
|
