129l: Difference between revisions

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==About this Structure==
==About this Structure==
129L is a [[Single protein]] structure of 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=129L OCA].  
129L is a 1 chain structure of 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=129L OCA].  


==Reference==
==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., Pjura P, Matthews BW, Protein Sci. 1993 Dec;2(12):2226-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8298466 8298466]
<ref group="xtra">PMID:8298466</ref><references group="xtra"/>
[[Category: Enterobacteria phage t4]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[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 Tue Feb 17 00:30:55 2009''

Revision as of 01:30, 17 February 2009

File:129l.png

Template:STRUCTURE 129l

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

129L is a 1 chain structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. 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

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