User:Shai Biran/Sandbox 310

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-==Shai's GFP page==
+==Yeast Eps1p==
 <StructureSection load='4TVE' size='340' side='right' caption='GFP' scene=''>
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 == Introduction ==
-Eps1p, a S. cerevisiae disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry [[4TVE]]). It is a unique member of the Protein Disulfide Isomerase family of proteins.
+Eps1p, a ''S. cerevisiae'' disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry [[4TVE]]). It is a unique member of the Protein Disulfide Isomerase family of proteins.
 == Exploring the Structure ==
-GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='61/612803/1ema_chromophore/1'>chromophore</scene>, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues<ref>PMID:8703075</ref>.
+Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='65/650818/Trx2-cxxc/1'>Trx2-CXXC</scene> is not solvent acceible, unlike any other CXXC motif in other Trx domains.