2fh0

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(New page: 200px<br /><applet load="2fh0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fh0" /> '''NMR Ensemble of The Yeast Saccharomyces cere...)
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[[Image:2fh0.jpg|left|200px]]<br /><applet load="2fh0" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR Ensemble of The Yeast Saccharomyces cerevisiae protein Ymr074cp core region'''<br />
'''NMR Ensemble of The Yeast Saccharomyces cerevisiae protein Ymr074cp core region'''<br />
==Overview==
==Overview==
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A set of 424 nonmembrane proteins from Methanobacterium, thermoautotrophicum were cloned, expressed and purified for structural, studies. Of these, approximately 20% were found to be suitable candidates, for X-ray crystallographic or NMR spectroscopic analysis without further, optimization of conditions, providing an estimate of the number of the, most accessible structural targets in the proteome. A retrospective, analysis of the experimental behavior of these proteins suggested some, simple relations between sequence and solubility, implying that data bases, of protein properties will be useful in optimizing high throughput, strategies. Of the first 10 structures determined, several provided clues, to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by, biochemical methods. This demonstrates that structural proteomics is, feasible and can play a central role in functional genomics.
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A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics.
==About this Structure==
==About this Structure==
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2FH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FH0 OCA].
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2FH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH0 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hong, J.J.]]
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[[Category: Hong, J J.]]
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[[Category: Shi, Y.Y.]]
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[[Category: Shi, Y Y.]]
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[[Category: Wu, J.H.]]
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[[Category: Wu, J H.]]
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[[Category: Zhang, J.H.]]
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[[Category: Zhang, J H.]]
[[Category: nmr ensemble]]
[[Category: nmr ensemble]]
[[Category: ymr074cp]]
[[Category: ymr074cp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:33:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:22 2008''

Revision as of 15:21, 21 February 2008


2fh0

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NMR Ensemble of The Yeast Saccharomyces cerevisiae protein Ymr074cp core region

Overview

A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics.

About this Structure

2FH0 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural proteomics of an archaeon., Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH, Nat Struct Biol. 2000 Oct;7(10):903-9. PMID:11017201

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