1c43

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[[Image:1c43.gif|left|200px]]
[[Image:1c43.gif|left|200px]]
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{{Structure
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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_1c43| PDB=1c43 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c43 OCA], [http://www.ebi.ac.uk/pdbsum/1c43 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c43 RCSB]</span>
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'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''
'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''
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[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
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[[Category: n-terminal]]
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[[Category: N-terminal]]
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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 12:18:23 2008''
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Revision as of 09:18, 2 May 2008

Template:STRUCTURE 1c43

MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES


Overview

To minutely understand the effect of foreign N-terminal residues on the conformational stability of human lysozyme, five mutant proteins were constructed: two had Met or Ala in place of the N-terminal Lys residue (K1M and K1A, respectively), and others had one additional residue, Met, Gly or Pro, to the N-terminal Lys residue (Met(-1), Gly(-1) and Pro(-1), respectively). The thermodynamic parameters for denaturation of these mutant proteins were examined by differential scanning calorimetry and were compared with that of the wild-type protein. Three mutants with the extra residue were significantly destabilized: the changes in unfolding Gibbs energy (DeltaDeltaG) were -9.1 to -12.2 kJ.mol-1. However, the stability of two single substitutions at the N-terminal slightly decreased; the DeltaDeltaG values were only -0.5 to -2.5 kJ.mol-1. The results indicate that human lysozyme is destabilized by an expanded N-terminal residue. The crystal structural analyses of K1M, K1A and Gly(-1) revealed that the introduction of a residue at the N-terminal of human lysozyme caused the destruction of hydrogen bond networks with ordered water molecules, resulting in the destabilization of the protein.

About this Structure

1C43 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:10561612 Page seeded by OCA on Fri May 2 12:18:23 2008

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