Sandbox 36: Difference between revisions

Papain consists of a single polypeptide chain of 212 amino acid residues.  As with all proteins, folding to form secondary and tertiary structures is largely determined by the interactions of the <scene name='Sandbox_36/Papain_hydrophobicity/1'>hydrophobic residues</scene> to exclude water.  55 of these residues form 7 <scene name='Sandbox_36/Papain_helices/1'>helices</scene> and 45 residues form 17 <scene name='Sandbox_36/Papain_sheets/1'>beta sheet</scene> strands.  Besides these structures, the secondary structure of papain is irregular.  The protein's tertiary structure consists of two domains divided by a cleft in which the active site resides.   

Papain has several methanol <scene name='Sandbox_36/Papain_ligands/1'>ligands</scene> associated with it.  Various residues on papain <scene name='Sandbox_36/Papain_ligands_fgj/1'>hydrogen bond</scene> to these methanol molecules (methanol molecules are shown in green and associated residues are shown in blue). <ref> http://www.pdb.org/pdb/explore.do?structureId=9PAP </ref>