Sandbox 36: Difference between revisions
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==Structure== | ==Structure== | ||
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/2'>hydrophobic residues</scene> to exclude water (hydrophobic residues shown in purple). The remaining residues are <scene name='Sandbox_36/Papain_polar_residues/1'>polar</scene>, some carrying a <scene name='Sandbox_36/Papain_polar_residues_acidic/1'>negative charge</scene> (acidic) at physiological pH, others a <scene name='Sandbox_36/Papain_polar_residues_basic/1'>positive charge</scene> (basic), the rest of the polar residues are neutral | Papain consists of a single polypeptide chain of 212 amino acid residues. 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. 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/2'>hydrophobic residues</scene> to exclude water (hydrophobic residues shown in purple). The remaining residues are <scene name='Sandbox_36/Papain_polar_residues/1'>polar</scene>, some carrying a <scene name='Sandbox_36/Papain_polar_residues_acidic/1'>negative charge</scene> (acidic) at physiological pH, others a <scene name='Sandbox_36/Papain_polar_residues_basic/1'>positive charge</scene> (basic), the rest of the polar residues are neutral. The protein's tertiary structure consists of two domains divided by a cleft in which the active site resides.<ref> http://www.pdb.org/pdb/explore.do?structureId=9PAP </ref> | ||
