1ymz
From Proteopedia
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[[Image:1ymz.gif|left|200px]] | [[Image:1ymz.gif|left|200px]] | ||
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'''CC45, An Artificial WW Domain Designed Using Statistical Coupling Analysis''' | '''CC45, An Artificial WW Domain Designed Using Statistical Coupling Analysis''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMZ OCA]. | |
==Reference== | ==Reference== | ||
Evolutionary information for specifying a protein fold., Socolich M, Lockless SW, Russ WP, Lee H, Gardner KH, Ranganathan R, Nature. 2005 Sep 22;437(7058):512-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16177782 16177782] | Evolutionary information for specifying a protein fold., Socolich M, Lockless SW, Russ WP, Lee H, Gardner KH, Ranganathan R, Nature. 2005 Sep 22;437(7058):512-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16177782 16177782] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Gardner, K H.]] | [[Category: Gardner, K H.]] | ||
[[Category: Lee, H.]] | [[Category: Lee, H.]] | ||
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[[Category: Russ, W P.]] | [[Category: Russ, W P.]] | ||
[[Category: Socolich, M.]] | [[Category: Socolich, M.]] | ||
| - | [[Category: | + | [[Category: Artificial protein]] |
| - | [[Category: | + | [[Category: Computational design]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:31:34 2008'' | |
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Revision as of 13:31, 3 May 2008
CC45, An Artificial WW Domain Designed Using Statistical Coupling Analysis
Overview
Classical studies show that for many proteins, the information required for specifying the tertiary structure is contained in the amino acid sequence. Here, we attempt to define the sequence rules for specifying a protein fold by computationally creating artificial protein sequences using only statistical information encoded in a multiple sequence alignment and no tertiary structure information. Experimental testing of libraries of artificial WW domain sequences shows that a simple statistical energy function capturing coevolution between amino acid residues is necessary and sufficient to specify sequences that fold into native structures. The artificial proteins show thermodynamic stabilities similar to natural WW domains, and structure determination of one artificial protein shows excellent agreement with the WW fold at atomic resolution. The relative simplicity of the information used for creating sequences suggests a marked reduction to the potential complexity of the protein-folding problem.
About this Structure
Full crystallographic information is available from OCA.
Reference
Evolutionary information for specifying a protein fold., Socolich M, Lockless SW, Russ WP, Lee H, Gardner KH, Ranganathan R, Nature. 2005 Sep 22;437(7058):512-8. PMID:16177782 Page seeded by OCA on Sat May 3 16:31:34 2008
