1s54: Difference between revisions
New page: left|200px<br /><applet load="1s54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s54, resolution 2.20Å" /> '''Thr24Ala Bacteriorho... |
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[[Image:1s54.jpg|left|200px]]<br /><applet load="1s54" size=" | [[Image:1s54.jpg|left|200px]]<br /><applet load="1s54" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1s54, resolution 2.20Å" /> | caption="1s54, resolution 2.20Å" /> | ||
'''Thr24Ala Bacteriorhodopsin'''<br /> | '''Thr24Ala Bacteriorhodopsin'''<br /> | ||
==Overview== | ==Overview== | ||
Hydrogen bonds involving a carbon donor are very common in protein structures, and energy calculations suggest that | Hydrogen bonds involving a carbon donor are very common in protein structures, and energy calculations suggest that Calpha-H...O hydrogen bonds could be about one-half the strength of traditional hydrogen bonds. It has therefore been proposed that these nontraditional hydrogen bonds could be a significant factor in stabilizing proteins, particularly membrane proteins as there is a low dielectric and no competition from water in the bilayer core. Nevertheless, this proposition has never been tested experimentally. Here, we report an experimental test of the significance of Calpha-H...O bonds for protein stability. Thr24 in bacteriorhodopsin, which makes an interhelical Calpha-H...O hydrogen bond to the Calpha of Ala51, was changed to Ala, Val, and Ser, and the thermodynamic stability of the mutants was measured. None of the mutants had significantly reduced stability. In fact, T24A was more stable than the wild-type protein by 0.6 kcal/mol. Crystal structures were determined for each of the mutants, and, while some structural changes were seen for T24S and T24V, T24A showed essentially no apparent structural alteration that could account for the increased stability. Thus, Thr24 appears to destabilize the protein rather than stabilize. Our results suggest that Calpha-H...O bonds are not a major contributor to protein stability. | ||
==About this Structure== | ==About this Structure== | ||
1S54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with RET as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1S54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S54 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bowie, J | [[Category: Bowie, J U.]] | ||
[[Category: Chamberlain, A | [[Category: Chamberlain, A K.]] | ||
[[Category: Faham, S.]] | [[Category: Faham, S.]] | ||
[[Category: Grosfeld, D.]] | [[Category: Grosfeld, D.]] | ||
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[[Category: membrane protein; bacteriorhodopsin; bicelle]] | [[Category: membrane protein; bacteriorhodopsin; bicelle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:06 2008'' | ||
Revision as of 15:58, 21 February 2008
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Thr24Ala Bacteriorhodopsin
OverviewOverview
Hydrogen bonds involving a carbon donor are very common in protein structures, and energy calculations suggest that Calpha-H...O hydrogen bonds could be about one-half the strength of traditional hydrogen bonds. It has therefore been proposed that these nontraditional hydrogen bonds could be a significant factor in stabilizing proteins, particularly membrane proteins as there is a low dielectric and no competition from water in the bilayer core. Nevertheless, this proposition has never been tested experimentally. Here, we report an experimental test of the significance of Calpha-H...O bonds for protein stability. Thr24 in bacteriorhodopsin, which makes an interhelical Calpha-H...O hydrogen bond to the Calpha of Ala51, was changed to Ala, Val, and Ser, and the thermodynamic stability of the mutants was measured. None of the mutants had significantly reduced stability. In fact, T24A was more stable than the wild-type protein by 0.6 kcal/mol. Crystal structures were determined for each of the mutants, and, while some structural changes were seen for T24S and T24V, T24A showed essentially no apparent structural alteration that could account for the increased stability. Thus, Thr24 appears to destabilize the protein rather than stabilize. Our results suggest that Calpha-H...O bonds are not a major contributor to protein stability.
About this StructureAbout this Structure
1S54 is a Single protein structure of sequence from Halobacterium salinarum with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
A C alpha-H...O hydrogen bond in a membrane protein is not stabilizing., Yohannan S, Faham S, Yang D, Grosfeld D, Chamberlain AK, Bowie JU, J Am Chem Soc. 2004 Mar 3;126(8):2284-5. PMID:14982414
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