1ouc
From Proteopedia
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'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT''' | '''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT''' | ||
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[[Category: Yamagata, Y.]] | [[Category: Yamagata, Y.]] | ||
[[Category: Yutani, K.]] | [[Category: Yutani, K.]] | ||
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| - | [[Category: | + | [[Category: Disease mutation]] |
| - | [[Category: | + | [[Category: Signal]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:17:24 2008'' | |
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Revision as of 01:17, 3 May 2008
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT
Overview
To clarify the contribution of the hydrophobic effect to the conformational stability of human lysozyme, a series of Val to Ala mutants were constructed. The thermodynamic parameters for the denaturation of these nine mutant proteins were determined using differential scanning calorimetry (DSC), and the crystal structures were solved at high resolution. The denaturation Gibbs energy (delta delta G) and enthalpy (delta delta H) values of the mutant proteins ranged from +2.2 to- 6.3 kJ/mol and from +7 to -17 kJ/mol, respectively. The structural analyses showed that the mutation site and/or the residues around it in some proteins shifted toward the created cavity, and the substitutions affected not only the mutations site but also other parts far from the site, although the structural changes were not as great. Correlation between the changes in the thermodynamic parameters and the structural features of mutant proteins was examined, including the five Ile to Val mutant human lysozymes [Takano et al. (1995) J. Mol. Biol. 254, 62-76]. There was no simple general correlation between delta delta G and the changes in hydrophobic surface area exposed upon denaturation (delta delta ASAHP). We found only a new correlation between the delta delta G and delta delta ASAHP of all of the hydrophobic residues if the effect of the secondary structure propensity was taken into account.
About this Structure
1OUC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants., Takano K, Yamagata Y, Fujii S, Yutani K, Biochemistry. 1997 Jan 28;36(4):688-98. PMID:9020766 Page seeded by OCA on Sat May 3 04:17:24 2008
Categories: Homo sapiens | Lysozyme | Single protein | Fujii, S. | Takano, K. | Yamagata, Y. | Yutani, K. | Amyloid | Disease mutation | Signal
