Lysin: Difference between revisions

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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>. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, 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. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.  


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Carmit Ginesin, Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman