1l18

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[[Image:1l18.jpg|left|200px]]<br /><applet load="1l18" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l18.jpg|left|200px]]
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caption="1l18, resolution 1.7&Aring;" />
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'''HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3'''<br />
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{{Structure
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|PDB= 1l18 |SIZE=350|CAPTION= <scene name='initialview01'>1l18</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE=
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}}
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'''HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1L18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA].
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1L18 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3405287 3405287]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/3405287 3405287]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:58 2008''

Revision as of 10:25, 20 March 2008

Image:1l18.jpg


PDB ID 1l18

Drag the structure with the mouse to rotate
, resolution 1.7Å
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 12:24:58 2008

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