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1l19

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[[Image:1l19.jpg|left|200px]]
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[[Image:1l19.png|left|200px]]
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{{STRUCTURE_1l19| PDB=1l19 | SCENE= }}
{{STRUCTURE_1l19| PDB=1l19 | SCENE= }}
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'''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''
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===ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES===
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==Overview==
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Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.
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(as it appears on PubMed at http://www.pubmed.gov), where 3200317 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3200317}}
==About this Structure==
==About this Structure==
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Nicholson, H.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:25:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:28:49 2008''

Revision as of 08:28, 2 July 2008

Image:1l19.png

Template:STRUCTURE 1l19

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

Template:ABSTRACT PUBMED 3200317

About this Structure

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

Reference

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317

Page seeded by OCA on Wed Jul 2 11:28:49 2008

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