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2v3l

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[[Image:2v3l.gif|left|200px]]
[[Image:2v3l.gif|left|200px]]
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{{Structure
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|PDB= 2v3l |SIZE=350|CAPTION= <scene name='initialview01'>2v3l</scene>
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The line below this paragraph, containing "STRUCTURE_2v3l", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=R6G:RHODAMINE+6G'>R6G</scene>
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{{STRUCTURE_2v3l| PDB=2v3l | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3l OCA], [http://www.ebi.ac.uk/pdbsum/2v3l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v3l RCSB]</span>
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'''ORIENTATIONAL AND DYNAMICAL HETEROGENEITY OF RHODAMINE 6G TERMINALLY ATTACHED TO A DNA HELIX'''
'''ORIENTATIONAL AND DYNAMICAL HETEROGENEITY OF RHODAMINE 6G TERMINALLY ATTACHED TO A DNA HELIX'''
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==About this Structure==
==About this Structure==
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2V3L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3L OCA].
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2V3L is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3L OCA].
==Reference==
==Reference==
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[[Category: Verdier, L.]]
[[Category: Verdier, L.]]
[[Category: Volkmer, A.]]
[[Category: Volkmer, A.]]
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[[Category: dna]]
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[[Category: Dna]]
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[[Category: nucleic acid]]
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[[Category: Nucleic acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:09:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:10 2008''
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Revision as of 15:09, 4 May 2008

Image:2v3l.gif

Template:STRUCTURE 2v3l

ORIENTATIONAL AND DYNAMICAL HETEROGENEITY OF RHODAMINE 6G TERMINALLY ATTACHED TO A DNA HELIX


Overview

The comparison of Forster resonance energy transfer (FRET) efficiencies between two fluorophores covalently attached to a single protein or DNA molecule is an elegant approach for deducing information about their structural and dynamical heterogeneity. For a more detailed structural interpretation of single-molecule FRET assays, information about the positions as well as the dynamics of the dye labels attached to the biomolecule is important. In this work, Rhodamine 6G (2-[3'-(ethylamino)-6'-(ethylimino)-2',7'-dimethyl-6'H-xanthen-9'-yl]-benz oic acid) bound to the 5'-end of a 20 base pair long DNA duplex is investigated by both single-molecule multiparameter fluorescence detection (MFD) experiments and NMR spectroscopy. Rhodamine 6G is commonly employed in nucleic acid research as a FRET dye. MFD experiments directly reveal the equilibrium of the dye bound to DNA between three heterogeneous environments, which are characterized by distinct fluorescence lifetime and intensity distributions as a result of different guanine-dye excited-state electron transfer interactions. Sub-ensemble fluorescence autocorrelation analysis shows the highly dynamic character of the dye-DNA interactions ranging from nano- to milliseconds and species-specific triplet relaxation times. Two-dimensional NMR spectroscopy corroborates this information by the determination of the detailed geometric structures of the dye-nucleobase complex and their assignment to each population observed in the single-molecule fluorescence experiments. From both methods, a consistent and detailed molecular description of the structural and dynamical heterogeneity is obtained.

About this Structure

2V3L is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Orientational and dynamical heterogeneity of rhodamine 6G terminally attached to a DNA helix revealed by NMR and single-molecule fluorescence spectroscopy., Neubauer H, Gaiko N, Berger S, Schaffer J, Eggeling C, Tuma J, Verdier L, Seidel CA, Griesinger C, Volkmer A, J Am Chem Soc. 2007 Oct 24;129(42):12746-55. Epub 2007 Sep 27. PMID:17900110 Page seeded by OCA on Sun May 4 18:09:33 2008

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