1uue: Difference between revisions
New page: left|200px<br /><applet load="1uue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uue, resolution 2.60Å" /> '''A-SPECTRIN SH3 DOMAI... |
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[[Image:1uue.jpg|left|200px]]<br /><applet load="1uue" size=" | [[Image:1uue.jpg|left|200px]]<br /><applet load="1uue" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1uue, resolution 2.60Å" /> | caption="1uue, resolution 2.60Å" /> | ||
'''A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)'''<br /> | '''A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)'''<br /> | ||
==Overview== | ==Overview== | ||
An effort to combine theoretical analyses and protein engineering methods | An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism. | ||
==About this Structure== | ==About this Structure== | ||
1UUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | 1UUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Fernandez, A.]] | [[Category: Fernandez, A.]] | ||
[[Category: Serrano, L.]] | [[Category: Serrano, L.]] | ||
[[Category: Vega, M | [[Category: Vega, M C.]] | ||
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
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[[Category: spectrin]] | [[Category: spectrin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:25 2008'' | ||
Revision as of 16:28, 21 February 2008
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A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)
OverviewOverview
An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism.
About this StructureAbout this Structure
1UUE is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Solvation in protein folding analysis: combination of theoretical and experimental approaches., Fernandez-Escamilla AM, Cheung MS, Vega MC, Wilmanns M, Onuchic JN, Serrano L, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2834-9. Epub 2004 Feb 20. PMID:14978284
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