Lysin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule<scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action. | + | The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule<scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action. |
Revision as of 21:48, 22 November 2014
egg lysin
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References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Carmit Ginesin, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
