1l20: Difference between revisions

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-[[Image:1l20.jpg|left|200px]]
+{{Seed}}
+[[Image:1l20.png|left|200px]]
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 {{STRUCTURE_1l20|  PDB=1l20  |  SCENE=  }}
-'''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''
+===ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_3200317}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3200317 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3200317}}
 ==About this Structure==
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 [[Category: Matthews, B W.]]
 [[Category: Nicholson, H.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:27:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:31:30 2008''

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