Sandbox 30: Difference between revisions

Line 17:

===Residue Distribution===

As can be seen from its <scene name='Sandbox_30/Papain_polarity_ballandstick/3'>ball and stick model</scene>, papain contains a variety of acidic (red), basic (blue), hydrophilic uncharged (pink), and hydrophobic (gray) residues. Since the enzyme operates in free solution, it would be expected that the hydrophilic residues would reside mostly on it exterior, shielding a hydrophobic core. This can be plainly seen from papain's <scene name='Sandbox_30/Papain_polarity_spacefill/3'>space filling model</scene>, in which hydrophilic residues are ~~purple~~ and hydrophobic residues are ~~grey~~. Upon removal of the hydrophilic residues, the <scene name='Sandbox_30/Papain_hydrophobic_spacefill/2'>hydrophobic core</scene> of the enzyme is easy to see. As with all proteins, it is this hydrophobic segregation that allows the protein to properly fold and maintain a meaningful shape.

As can be seen from its <scene name='Sandbox_30/Papain_polarity_ballandstick/3'>ball and stick model</scene>, papain contains a variety of acidic (red), basic (blue), hydrophilic uncharged (pink), and hydrophobic (gray) residues. Since the enzyme operates in free solution, it would be expected that the hydrophilic residues would reside mostly on it exterior, shielding a hydrophobic core. This can be plainly seen from papain's <scene name='Sandbox_30/Papain_polarity_spacefill/4'>space filling model</scene>, in which hydrophilic residues are pink and hydrophobic residues are orange. Upon removal of the hydrophilic residues, the <scene name='Sandbox_30/Papain_hydrophobic_spacefill/3'>hydrophobic core</scene> of the enzyme is easy to see. As with all proteins, it is this hydrophobic segregation that allows the protein to properly fold and maintain a meaningful shape.

===Ligands===

Sandbox 30: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 17: / Line 17: @@
 ===Residue Distribution===
-As can be seen from its <scene name='Sandbox_30/Papain_polarity_ballandstick/3'>ball and stick model</scene>, papain contains a variety of acidic (red), basic (blue), hydrophilic uncharged (pink), and hydrophobic (gray) residues.  Since the enzyme operates in free solution, it would be expected that the hydrophilic residues would reside mostly on it exterior, shielding a hydrophobic core.  This can be plainly seen from papain's <scene name='Sandbox_30/Papain_polarity_spacefill/3'>space filling model</scene>, in which hydrophilic residues are purple and hydrophobic residues are grey.  Upon removal of the hydrophilic residues, the <scene name='Sandbox_30/Papain_hydrophobic_spacefill/2'>hydrophobic core</scene> of the enzyme is easy to see.  As with all proteins, it is this hydrophobic segregation that allows the protein to properly fold and maintain a meaningful shape.
+As can be seen from its <scene name='Sandbox_30/Papain_polarity_ballandstick/3'>ball and stick model</scene>, papain contains a variety of acidic (red), basic (blue), hydrophilic uncharged (pink), and hydrophobic (gray) residues.  Since the enzyme operates in free solution, it would be expected that the hydrophilic residues would reside mostly on it exterior, shielding a hydrophobic core.  This can be plainly seen from papain's <scene name='Sandbox_30/Papain_polarity_spacefill/4'>space filling model</scene>, in which hydrophilic residues are pink and hydrophobic residues are orange.  Upon removal of the hydrophilic residues, the <scene name='Sandbox_30/Papain_hydrophobic_spacefill/3'>hydrophobic core</scene> of the enzyme is easy to see.  As with all proteins, it is this hydrophobic segregation that allows the protein to properly fold and maintain a meaningful shape.
 ===Ligands===