1wqq

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[[Image:1wqq.gif|left|200px]]
[[Image:1wqq.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1wqq |SIZE=350|CAPTION= <scene name='initialview01'>1wqq</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1wqq", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1wqq| PDB=1wqq | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqq OCA], [http://www.ebi.ac.uk/pdbsum/1wqq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wqq RCSB]</span>
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}}
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'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME'''
'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME'''
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[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
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[[Category: bacteriolytic enzyme]]
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[[Category: Bacteriolytic enzyme]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:01:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:48 2008''
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Revision as of 11:01, 3 May 2008

Image:1wqq.gif

Template:STRUCTURE 1wqq

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME


Overview

The contribution of hydrogen bonds to the conformational stability of human lysozyme was investigated by the combination of calorimetric and X-ray analyses of six Tyr --> Phe mutants. Unfolding Delta G and unfolding Delta H values of the Tyr --> Phe mutant proteins were changed by from +0.3 to -4.0 kJ/mol and from 0 to -16 kJ/mol, respectively, compared to those of the wild-type protein. The net contribution of a hydrogen bond at a specific site to stability (Delta Gwild/HB), considering factors affected by substitutions, was evaluated on the basis of X-ray structures of the mutant proteins. In the present study, one of six mutant proteins was suitable for evaluating the strength of the hydrogen bond. Delta Gwild/HB for the intramolecular hydrogen bond at Tyr124 was evaluated to be 7.5 kJ/mol. Results of the analysis of other mutants also suggest that hydrogen bonds of the hydroxyl group of Tyr, including the hydrogen bond with a water molecule, contribute to the stabilization of the human lysozyme.

About this Structure

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

Reference

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants., Yamagata Y, Kubota M, Sumikawa Y, Funahashi J, Takano K, Fujii S, Yutani K, Biochemistry. 1998 Jun 30;37(26):9355-62. PMID:9649316 Page seeded by OCA on Sat May 3 14:01:27 2008

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