130l
From Proteopedia
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===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=== | ===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=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[130l]] is a 1 chain structure of [[Hen Egg-White (HEW) Lysozyme]] 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]. | |
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| + | ==See Also== | ||
| + | *[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008298466</ref><references group="xtra"/> |
[[Category: Enterobacteria phage t4]] | [[Category: Enterobacteria phage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Pjura, P.]] | [[Category: Pjura, P.]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 20 08:45:58 2010'' | ||
Revision as of 21:08, 26 July 2012
Contents |
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
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
