Sandbox 36: Difference between revisions

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==Structure==

Papain consists of a single polypeptide chain of 212 amino acid residues split into two lobes. 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). A majority of these hydrophobic residues form hydrophobic cores within each of the lobes ensuring their stability (surface residues are transparent, buried hydrophobic residues are opaque and colored). 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>

Papain consists of a single polypeptide chain of 212 amino acid residues split into two lobes. 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). A majority of these hydrophobic residues form <scene name='Sandbox_36/Papain_hydrophobic_cores/1'>hydrophobic cores</scene> within each of the lobes ensuring their stability (surface residues are transparent, buried hydrophobic residues are opaque and colored). 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>

Sandbox 36: Difference between revisions

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Revision as of 10:24, 13 March 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 10:31, 13 March 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	==Structure==		==Structure==
	Papain consists of a single polypeptide chain of 212 amino acid residues split into two lobes. 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). A majority of these hydrophobic residues form hydrophobic cores within each of the lobes ensuring their stability (surface residues are transparent, buried hydrophobic residues are opaque and colored). 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>		Papain consists of a single polypeptide chain of 212 amino acid residues split into two lobes. 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). A majority of these hydrophobic residues form <scene name='Sandbox_36/Papain_hydrophobic_cores/1'>hydrophobic cores</scene> within each of the lobes ensuring their stability (surface residues are transparent, buried hydrophobic residues are opaque and colored). 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>