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1l19
From Proteopedia
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
1L19 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 Fri May 2 23:25:38 2008
