1c43: Difference between revisions

Revision as of 20:11, 30 June 2008

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File:1c43.png

Template:STRUCTURE 1c43

MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUESMUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

Template:ABSTRACT PUBMED 10561612

About this StructureAbout this Structure

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

ReferenceReference

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

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-'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''
+===MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10561612}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10561612}}
 ==About this Structure==
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 [[Category: N-terminal]]
 [[Category: Stability]]
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