1b5w: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1b5w.gif|left|200px]]
[[Image:1b5w.gif|left|200px]]


{{Structure
<!--
|PDB= 1b5w |SIZE=350|CAPTION= <scene name='initialview01'>1b5w</scene>, resolution 2.17&Aring;
The line below this paragraph, containing "STRUCTURE_1b5w", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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=  
-->
|DOMAIN=
{{STRUCTURE_1b5w| PDB=1b5w  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5w OCA], [http://www.ebi.ac.uk/pdbsum/1b5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5w RCSB]</span>
}}


'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS'''
'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS'''
Line 32: Line 29:
[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
[[Category: hydrogen bond]]
[[Category: Hydrogen bond]]
[[Category: stability]]
[[Category: Stability]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:06:35 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:16 2008''

Revision as of 11:06, 2 May 2008

File:1b5w.gif

Template:STRUCTURE 1b5w

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS


OverviewOverview

To further examine the contribution of hydrogen bonds to the conformational stability of the human lysozyme, six Ser to Ala mutants were constructed. The thermodynamic parameters for denaturation of these six Ser mutant proteins were investigated by differential scanning calorimetry (DSC), and the crystal structures were determined by X-ray analysis. The denaturation Gibbs energy (DeltaG) of the Ser mutant proteins was changed from 2.0 to -5.7 kJ/mol, compared to that of the wild-type protein. With an analysis in which some factors that affected the stability due to mutation were considered, the contribution of hydrogen bonds to the stability (Delta DeltaGHB) was extracted on the basis of the structures of the mutant proteins. The results showed that hydrogen bonds between protein atoms and between a protein atom and a water bound with the protein molecule favorably contribute to the protein stability. The net contribution of one intramolecular hydrogen bond to protein stability (DeltaGHB) was 8.9 +/- 2.6 kJ/mol on average. However, the contribution to the protein stability of hydrogen bonds between a protein atom and a bound water molecule was smaller than that for a bond between protein atoms.

About this StructureAbout this Structure

1B5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants., Takano K, Yamagata Y, Kubota M, Funahashi J, Fujii S, Yutani K, Biochemistry. 1999 May 18;38(20):6623-9. PMID:10350481 Page seeded by OCA on Fri May 2 11:06:35 2008

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

OCA