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1l20

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Revision as of 18:56, 30 March 2008 by OCA (Talk | contribs)
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Image:1l20.jpg


PDB ID 1l20

Drag the structure with the mouse to rotate
, resolution 1.85Å
Activity: Lysozyme, with EC number 3.2.1.17
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES


Overview

Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.

About this Structure

1L20 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317

Page seeded by OCA on Sun Mar 30 21:56:52 2008

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