Lysin: Difference between revisions

← Older edit Newer edit →

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

Revision as of 00:46, 23 November 2014 view source Carmit Ginesin (talk \| contribs) 87 edits No edit summary ← Older edit		Revision as of 00:48, 23 November 2014 view source Carmit Ginesin (talk \| contribs) 87 edits No edit summary Newer edit →
Line 9:		Line 9:

	== 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.