1ip7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ip7.jpg|left|200px]] | [[Image:1ip7.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1ip7", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1ip7| PDB=1ip7 | SCENE= }} | ||
}} | |||
'''G129A HUMAN LYSOZYME''' | '''G129A HUMAN LYSOZYME''' | ||
| Line 29: | Line 26: | ||
[[Category: Yamagata, Y.]] | [[Category: Yamagata, Y.]] | ||
[[Category: Yutani, K.]] | [[Category: Yutani, K.]] | ||
[[Category: | [[Category: Bacteriolytic enzyme]] | ||
[[Category: | [[Category: Glycosidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:14:53 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:14, 2 May 2008
G129A HUMAN LYSOZYME
OverviewOverview
Our previous study of six non-Gly to Gly/Ala mutant human lysozymes in a left-handed helical region showed that only one non-Gly residue at a rigid site had unfavorable strain energy as compared with Gly at the same position (Takano et al., Proteins 2001; 44:233-243). To further examine the role of left-handed residues in the conformational stability of a protein, we constructed ten Gly to Ala mutant human lysozymes. Most Gly residues in human lysozyme are located in the left-handed helix region. The thermodynamic parameters for denaturation and crystal structures were determined by differential scanning calorimetry and X-ray analysis, respectively. The difference in denaturation Gibbs energy (DeltaDeltaG) for the ten Gly to Ala mutants ranged from + 1.9 to -7.5 kJ/mol, indicating that the effect of the mutation depends on the environment of the residue. We confirm that Gly in a left-handed region is more favorable at rigid sites than non-Gly, but there is little difference in energetic cost between Gly and non-Gly at flexible sites. The present results indicate that dihedral angles in the backbone conformation and also the flexibility at the position should be considered for analyses of protein stability, and protein structural determination, prediction, and design.
About this StructureAbout this Structure
1IP7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein., Takano K, Yamagata Y, Yutani K, Proteins. 2001 Nov 15;45(3):274-80. PMID:11599030 Page seeded by OCA on Fri May 2 20:14:53 2008