2hee: Difference between revisions

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[[Image:2hee.jpg|left|200px]]
[[Image:2hee.jpg|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_2hee", creates the "Structure Box" on the page.
|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
or leave the SCENE parameter empty for the default display.
|GENE= HUMAN LYSOZYME WITH ILE 59 REP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2hee| PDB=2hee  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hee OCA], [http://www.ebi.ac.uk/pdbsum/2hee PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hee RCSB]</span>
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'''CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''
'''CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''
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[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
[[Category: glycosidase]]
[[Category: Glycosidase]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: o-glycosyl]]
[[Category: O-glycosyl]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:29:12 2008''

Revision as of 06:11, 4 May 2008

File:2hee.jpg

Template:STRUCTURE 2hee

CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY


OverviewOverview

Water molecules frequently occur in the interior of globular proteins. To elucidate the contribution of buried water molecules to the conformational stability of a protein, we examined the crystal structures and the thermodynamic parameters of denaturation of six Ile to Ala/Gly mutant human lysozymes, in which a cavity is created at each mutation site by the substitution of a smaller side-chain for a larger one. One or two ordered water molecules were found in the cavities created in some mutants (I106A, I59A and I59G). The cavity volumes for these three mutants were bigger than those that remained empty in the other mutants. The stability of the mutant proteins with the newly introduced water molecules was about 8 kJ/mol higher than that expected from the change in hydrophobic surface area (DeltaDeltaASAHP) exposed upon denaturation. It was concluded that a water molecule in a cavity created in the interior of a protein contributes favorably to the stability.

About this StructureAbout this Structure

2HEE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Contribution of water molecules in the interior of a protein to the conformational stability., Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K, J Mol Biol. 1997 Nov 21;274(1):132-42. PMID:9398521 Page seeded by OCA on Sun May 4 06:11:16 2008

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