1qes: Difference between revisions
New page: left|200px<br /><applet load="1qes" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qes" /> '''TANDEM GU MISMATCHES IN RNA, NMR, 30 STRUCTU... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qes.gif|left|200px]]<br /><applet load="1qes" size=" | [[Image:1qes.gif|left|200px]]<br /><applet load="1qes" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qes" /> | caption="1qes" /> | ||
'''TANDEM GU MISMATCHES IN RNA, NMR, 30 STRUCTURES'''<br /> | '''TANDEM GU MISMATCHES IN RNA, NMR, 30 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
The symmetric, tandem GU mismatch motifs, and , which only differ in the | The symmetric, tandem GU mismatch motifs, and , which only differ in the mismatch order, have an average difference in thermodynamic stability of 2 kcal/mol at 37 degrees C. Thermodynamic studies of duplexes containing these motifs indicate the effect is largely localized to the mismatches and adjacent base pairs. The three-dimensional structures of two representative duplexes, (rGGAGUUCC)2 and (rGGAUGUCC)2, were determined by two-dimensional NMR and a simulated annealing protocol. Local deviations are similar to other intrahelical GU mismatches with little effect on backbone torsion angles and a slight overtwisting between the base pair 5' of the G of the mismatch and the mismatch itself. Comparisons of the resulting stacking patterns along with electrostatic potential maps suggest that interactions between highly negative electrostatic regions between base pairs may play a role in the observed thermodynamic differences. | ||
==About this Structure== | ==About this Structure== | ||
1QES 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:// | 1QES 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=1QES OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Chen, X.]] | [[Category: Chen, X.]] | ||
[[Category: He, L.]] | [[Category: He, L.]] | ||
[[Category: Mcdowell, J | [[Category: Mcdowell, J A.]] | ||
[[Category: Turner, D | [[Category: Turner, D H.]] | ||
[[Category: g:u mismatch]] | [[Category: g:u mismatch]] | ||
[[Category: ribonucleic acid]] | [[Category: ribonucleic acid]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:40 2008'' | ||
Revision as of 15:38, 21 February 2008
|
TANDEM GU MISMATCHES IN RNA, NMR, 30 STRUCTURES
OverviewOverview
The symmetric, tandem GU mismatch motifs, and , which only differ in the mismatch order, have an average difference in thermodynamic stability of 2 kcal/mol at 37 degrees C. Thermodynamic studies of duplexes containing these motifs indicate the effect is largely localized to the mismatches and adjacent base pairs. The three-dimensional structures of two representative duplexes, (rGGAGUUCC)2 and (rGGAUGUCC)2, were determined by two-dimensional NMR and a simulated annealing protocol. Local deviations are similar to other intrahelical GU mismatches with little effect on backbone torsion angles and a slight overtwisting between the base pair 5' of the G of the mismatch and the mismatch itself. Comparisons of the resulting stacking patterns along with electrostatic potential maps suggest that interactions between highly negative electrostatic regions between base pairs may play a role in the observed thermodynamic differences.
About this StructureAbout this Structure
1QES is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Investigation of the structural basis for thermodynamic stabilities of tandem GU wobble pairs: NMR structures of (rGGAGUUCC)2 and (rGGAUGUCC)2., McDowell JA, He L, Chen X, Turner DH, Biochemistry. 1997 Jul 1;36(26):8030-8. PMID:9201950
Page seeded by OCA on Thu Feb 21 14:38:40 2008