1s53: Difference between revisions

Revision as of 03:50, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s53.png

Template:STRUCTURE 1s53

Thr46Ser BacteriorhodopsinThr46Ser Bacteriorhodopsin

Template:ABSTRACT PUBMED 14982414

About this StructureAbout this Structure

1S53 is a Single protein structure of sequence from Halobacterium salinarum. 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

Page seeded by OCA on Mon Jul 28 03:50:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1s53.jpg|left|200px]]
+{{Seed}}
+[[Image:1s53.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1s53|  PDB=1s53  |  SCENE=  }}
-'''Thr46Ser Bacteriorhodopsin'''
+===Thr46Ser Bacteriorhodopsin===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14982414}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14982414 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14982414}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Bicelle]]
 [[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:18:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:50:08 2008''