1l18

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(New page: 200px<br /><applet load="1l18" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l18, resolution 1.7&Aring;" /> '''HYDROPHOBIC STABILIZA...)
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Revision as of 18:02, 20 November 2007

Image:1l18.jpg

1l18, resolution 1.7Å

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HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3

Overview

Replacing the isoleucine at amino-acid position three of bacteriophage T4, lysozyme causes changes in the thermodynamic stability of the protein that, are directly related to the hydrophobicity of the substituted residue., Structural analysis confirms that the hydrophobic stabilization is, proportional to the reduction of the surface area accessible to solvent on, folding.

About this Structure

1L18 is a Single protein structure of sequence from Bacteriophage t4. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3., Matsumura M, Becktel WJ, Matthews BW, Nature. 1988 Aug 4;334(6181):406-10. PMID:3405287

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