1s1o

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(New page: 200px<br /><applet load="1s1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s1o" /> '''NMR Structure of a D,L Alternating pentadeca...)
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[[Image:1s1o.jpg|left|200px]]<br /><applet load="1s1o" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix'''<br />
'''NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1S1O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with BOC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S1O OCA].
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1S1O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=BOC:'>BOC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1O OCA].
==Reference==
==Reference==
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[[Category: norleucine]]
[[Category: norleucine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:42:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:00 2008''

Revision as of 12:57, 21 February 2008

Image:1s1o.jpg

1s1o

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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 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

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