1l18: Difference between revisions

Revision as of 23:25, 2 May 2008

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

OverviewOverview

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 StructureAbout this Structure

1L18 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

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 Fri May 2 23:25:33 2008

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OCA

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 [[Image:1l18.jpg|left|200px]]
- {{Structure
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-}}
 '''HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3'''
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 [[Category: Matsumura, M.]]
 [[Category: Matthews, B W.]]
-[[Category: hydrolase (o-glycosyl)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:25:33 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:32 2008''