Sandbox 38

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. Papain spinqualitylabelsall models == Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D composition of the enzyme</scene> can be view, as carbon is labled gray, oxygen red, nitrogen blue, and sulfur yellow. There are three disulfide bridges that contribute to the structure of Papain. These bonds are indicated by their yellow color, as they link particular cysteine residues. Throughout this enzyme, there are specific charged residues, indicating the most polar portions of the molecule. These charged residues can be visualized, as the cationic residues are blue in color, while the anionic residues are red. Partially charged residues are simply lighter in color. It is interesting to note that nearly all of these charged residues are located on the outer portion of the molecule in order to interact with the surrounding environment. Hydrophobicity and Hydrophilicity: These charged residues contribute to the overall hydrophobicity (water hating) and hydrophilicity (water loving) portions of the enzyme, as the hydrophobic and hydrophilic regions are a huge factor in determining protein folding. As mentioned before, the charged, hydrophilic, portions of the enzyme are primarily located on the out portion of the molecule. The polar amino acids are indicated by a purple color, while the hydrophobic residues are gray. ligands of Papain Hydrophobic Residues.