1e8j: Difference between revisions

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'''SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES'''<br />
{{Structure
|PDB= 1e8j |SIZE=350|CAPTION= <scene name='initialview01'>1e8j</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1E8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8J OCA].  
1E8J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8J OCA].  


==Reference==
==Reference==
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes., Lamosa P, Brennan L, Vis H, Turner DL, Santos H, Extremophiles. 2001 Oct;5(5):303-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11699644 11699644]
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes., Lamosa P, Brennan L, Vis H, Turner DL, Santos H, Extremophiles. 2001 Oct;5(5):303-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11699644 11699644]
[[Category: Desulfovibrio gigas]]
[[Category: Desulfovibrio gigas]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc-substitution]]
[[Category: zinc-substitution]]


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Revision as of 11:51, 20 March 2008

File:1e8j.jpg


PDB ID 1e8j

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SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES


OverviewOverview

Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/-0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.

About this StructureAbout this Structure

1E8J is a Single protein structure of sequence from Desulfovibrio gigas. Full crystallographic information is available from OCA.

ReferenceReference

NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes., Lamosa P, Brennan L, Vis H, Turner DL, Santos H, Extremophiles. 2001 Oct;5(5):303-11. PMID:11699644

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