1l20 | pdb_00001l20

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Template:STRUCTURE 1l20

File:1l20.png

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

Template:ABSTRACT PUBMED 3200317

About this Structure

1L20 is a 1 chain structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

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:https://dx.doi.org/10.1038/336651a0

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[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:https://dx.doi.org/10.1038/336651a0

1l20 | pdb_00001l20

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

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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