129l: Difference between revisions

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[[Image:129l.jpg|left|200px]]<br /><applet load="129l" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:129l.jpg|left|200px]]
caption="129l, resolution 1.7&Aring;" />
 
'''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'''<br />
{{Structure
|PDB= 129l |SIZE=350|CAPTION= <scene name='initialview01'>129l</scene>, resolution 1.7&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
|GENE=
}}
 
'''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'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
129L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=129L OCA].  
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].  


==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8298466 8298466]
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]
[[Category: Enterobacteria phage t4]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase(o-glycosyl)]]
[[Category: hydrolase(o-glycosyl)]]


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