130l: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
[[130l]] is a 1 chain structure | [[130l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=130L OCA]. | ||
==See Also== | ==See Also== | ||
Revision as of 19:16, 20 October 2012
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 SOLVENTSTRUCTURES 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 StructureAbout this Structure
130l is a 1 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ 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