1kxx

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[[Image:1kxx.gif|left|200px]]
[[Image:1kxx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1kxx |SIZE=350|CAPTION= <scene name='initialview01'>1kxx</scene>, resolution 1.71&Aring;
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The line below this paragraph, containing "STRUCTURE_1kxx", 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=
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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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or leave the SCENE parameter empty for the default display.
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|GENE= HEN LYSOZYME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
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|DOMAIN=
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{{STRUCTURE_1kxx| PDB=1kxx | 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=1kxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kxx OCA], [http://www.ebi.ac.uk/pdbsum/1kxx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kxx RCSB]</span>
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}}
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'''ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS'''
'''ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS'''
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[[Category: Ohmura, T.]]
[[Category: Ohmura, T.]]
[[Category: Ueda, T.]]
[[Category: Ueda, T.]]
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[[Category: electrostatic interaction]]
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[[Category: Electrostatic interaction]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: helix]]
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[[Category: Helix]]
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[[Category: hen lysozyme]]
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[[Category: Hen lysozyme]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: stability]]
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[[Category: Stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:18:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:19 2008''
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Revision as of 20:18, 2 May 2008

Image:1kxx.gif

Template:STRUCTURE 1kxx

ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS


Overview

In the N-terminal region of the alpha-helix of the c-type lysozymes, two Asx residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27 (18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type (18D/27N) lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the alpha-helix, while the stability of the 18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B-helix in 18D/27D lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein.

About this Structure

1KXX is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction., Motoshima H, Mine S, Masumoto K, Abe Y, Iwashita H, Hashimoto Y, Chijiiwa Y, Ueda T, Imoto T, J Biochem. 1997 Jun;121(6):1076-81. PMID:9354379 Page seeded by OCA on Fri May 2 23:18:27 2008

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