1osr
From Proteopedia
(New page: 200px<br /><applet load="1osr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osr" /> '''Structural study of dna duplex containaing a...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1osr.gif|left|200px]]<br /><applet load="1osr" size=" | + | [[Image:1osr.gif|left|200px]]<br /><applet load="1osr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1osr" /> | caption="1osr" /> | ||
'''Structural study of dna duplex containaing a n-(2-deoxy-beta-erytho-pentofuranosyl) formamide frameshift by nmr and restrained molecular dynamics'''<br /> | '''Structural study of dna duplex containaing a n-(2-deoxy-beta-erytho-pentofuranosyl) formamide frameshift by nmr and restrained molecular dynamics'''<br /> | ||
==Overview== | ==Overview== | ||
- | The presence of an N-(2-deoxy-beta-D-erythro-pentofuranosyl) formamide (F) | + | The presence of an N-(2-deoxy-beta-D-erythro-pentofuranosyl) formamide (F) residue, a ring fragmentation product of thymine, in a frameshift context in the sequence 5'-d-(AGGACCACG)*d(CGTGGFTCCT) has been studied by 1H and 31P nuclear magnetic resonance (NMR) and molecular dynamics. Two-dimensional NMR studies show that the formamide residue, whether the cis or trans isomer, is rotated out of the helix and that the bases on either side of the formamide residue in the sequence, G14 and T16, are stacked over each other in a way similar to normal B-DNA. The cis and trans isomers were observed in the ratio 3:2 in solution. Information extracted from 31P NMR data reveal a modification of the phosphodiester backbone conformation at the extrahelical site, which is also observed during the molecular dynamics simulations. |
==About this Structure== | ==About this Structure== | ||
- | 1OSR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1OSR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSR OCA]. |
==Reference== | ==Reference== | ||
Line 14: | Line 14: | ||
[[Category: Boulard, Y.]] | [[Category: Boulard, Y.]] | ||
[[Category: Cadet, J.]] | [[Category: Cadet, J.]] | ||
- | [[Category: Fazakerley, G | + | [[Category: Fazakerley, G V.]] |
[[Category: Maufrais, C.]] | [[Category: Maufrais, C.]] | ||
[[Category: deoxyribonucleic acid]] | [[Category: deoxyribonucleic acid]] | ||
Line 20: | Line 20: | ||
[[Category: mutagenesis]] | [[Category: mutagenesis]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:10 2008'' |
Revision as of 12:21, 21 February 2008
|
Structural study of dna duplex containaing a n-(2-deoxy-beta-erytho-pentofuranosyl) formamide frameshift by nmr and restrained molecular dynamics
Overview
The presence of an N-(2-deoxy-beta-D-erythro-pentofuranosyl) formamide (F) residue, a ring fragmentation product of thymine, in a frameshift context in the sequence 5'-d-(AGGACCACG)*d(CGTGGFTCCT) has been studied by 1H and 31P nuclear magnetic resonance (NMR) and molecular dynamics. Two-dimensional NMR studies show that the formamide residue, whether the cis or trans isomer, is rotated out of the helix and that the bases on either side of the formamide residue in the sequence, G14 and T16, are stacked over each other in a way similar to normal B-DNA. The cis and trans isomers were observed in the ratio 3:2 in solution. Information extracted from 31P NMR data reveal a modification of the phosphodiester backbone conformation at the extrahelical site, which is also observed during the molecular dynamics simulations.
About this Structure
1OSR is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structural study of DNA duplex containing an N-(2-deoxy-beta-D-erythro-pentofuranosyl) formamide frameshift by NMR and restrained molecular dynamics., Maufrais C, Fazakerley GV, Cadet J, Boulard Y, Nucleic Acids Res. 2003 Oct 15;31(20):5930-40. PMID:14530441
Page seeded by OCA on Thu Feb 21 14:21:10 2008