This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2v3l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v3l.gif|left|200px]]<br /><applet load="2v3l" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2v3l.gif|left|200px]]
-
caption="2v3l" />
+
 
-
'''ORIENTATIONAL AND DYNAMICAL HETEROGENEITY OF RHODAMINE 6G TERMINALLY ATTACHED TO A DNA HELIX'''<br />
+
{{Structure
 +
|PDB= 2v3l |SIZE=350|CAPTION= <scene name='initialview01'>2v3l</scene>
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=R6G:RHODAMINE 6G'>R6G</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''ORIENTATIONAL AND DYNAMICAL HETEROGENEITY OF RHODAMINE 6G TERMINALLY ATTACHED TO A DNA HELIX'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2V3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=R6G:'>R6G</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3L OCA].
+
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].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17900110 17900110]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/17900110 17900110]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berger, S.]]
[[Category: Berger, S.]]
Line 26: Line 35:
[[Category: nucleic acid]]
[[Category: nucleic acid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:57 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:42:55 2008''

Revision as of 16:42, 20 March 2008


PDB ID 2v3l

Drag the structure with the mouse to rotate
Ligands:
Coordinates: save as pdb, mmCIF, xml



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 of sequence from [1]. 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 Thu Mar 20 18:42:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools