131l

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File:131l.png

Template:STRUCTURE 131l

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

131L is a 1 chain structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 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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OCA

[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

[xtra 1]

131l

About this StructureAbout this Structure

ReferenceReference

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