130l

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Revision as of 21:08, 26 July 2012

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Template:STRUCTURE 130l

Contents 1 STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT 2 About this Structure 3 See Also 4 Reference

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

Template:ABSTRACT PUBMED 8298466

About this Structure

130l is a 1 chain structure of Hen Egg-White (HEW) Lysozyme with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

See Also

• Hen Egg-White (HEW) Lysozyme

Reference

• Pjura P, Matthews BW. Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. Protein Sci. 1993 Dec;2(12):2226-32. PMID:8298466 doi:http://dx.doi.org/10.1002/pro.5560021222