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| {{STRUCTURE_1c45| PDB=1c45 | SCENE= }} | | {{STRUCTURE_1c45| PDB=1c45 | SCENE= }} |
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| '''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''
| | ===MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES=== |
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| ==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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10561612 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10561612}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: N-terminal]] | | [[Category: N-terminal]] |
| [[Category: Stability]] | | [[Category: Stability]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:18:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:11:05 2008'' |
