3cod: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,327,076 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,327,076 edits
No edit summary
Line 1: Line 1:
[[Image:3cod.jpg|left|200px]]
{{Seed}}
[[Image:3cod.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3cod|  PDB=3cod  |  SCENE=  }}  
{{STRUCTURE_3cod|  PDB=3cod  |  SCENE=  }}  


'''Crystal Structure of T90A/D115A mutant of Bacteriorhodopsin'''
===Crystal Structure of T90A/D115A mutant of Bacteriorhodopsin===




==Overview==
<!--
Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis, that the average contribution of eight interhelical side-chain hydrogen-bonding interactions throughout bacteriorhodopsin is only 0.6 kcal mol(-1). In agreement with these experiments, we find that 4% of polar atoms in the non-polar core regions of membrane proteins have no hydrogen-bond partner and the lengths of buried hydrogen bonds in soluble proteins and membrane protein transmembrane regions are statistically identical. Our results indicate that most hydrogen-bond interactions in membrane proteins are only modestly stabilizing. Weak hydrogen-bonding should be reflected in considerations of membrane protein folding, dynamics, design, evolution and function.
The line below this paragraph, {{ABSTRACT_PUBMED_18500332}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18500332 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18500332}}


==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 10:02:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 9 10:11:17 2008''

Revision as of 07:11, 9 July 2008

File:3cod.png

Template:STRUCTURE 3cod

Crystal Structure of T90A/D115A mutant of Bacteriorhodopsin

Template:ABSTRACT PUBMED 18500332

About this Structure

3COD is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

Reference

Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins., Joh NH, Min A, Faham S, Whitelegge JP, Yang D, Woods VL, Bowie JU, Nature. 2008 May 25;. PMID:18500332

Page seeded by OCA on Wed Jul 9 10:11:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3cod&oldid=637537"