1l19

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Template:STRUCTURE 1l19

File:1l19.png

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLESENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES

Template:ABSTRACT PUBMED 3200317

About this StructureAbout this Structure

1L19 is a 1 chain structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Nicholson H, Becktel WJ, Matthews BW. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317 doi:http://dx.doi.org/10.1038/336651a0

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OCA

[1] Nicholson H, Becktel WJ, Matthews BW. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317 doi:http://dx.doi.org/10.1038/336651a0

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