Sandbox 33: Difference between revisions

In aqueous, physiological environments the <scene name='Sandbox_33/Stickwire_hydrophobic/1'>hydrophobic residues</scene> of adenylate kinase, seen in grey, are buried in the interior of the protein. The hydrophobic residues cluster together in the interior of the protein in order to avoid the exterior aqueous environment.  

The <scene name='Sandbox_33/Stickwire_charged/1'>hydrophilic</scene> polar and charged residues, seen in yellow, are found on the exterior of adenylate kinase.  It might be easier to visualize in <scene name='Sandbox_33/Hydrophilic_better/1'>this</scene> depiction of adenylate kinase, where the hydrophilic residues are depicted in red.  Hydrophilic residues are on the exterior of the protein because they can interact with the aqueous exterior environment.  Hydrophilic residues can exist on the interior of a protein by interacting solely with one another and avoiding interaction with hydrophobic residues.  Hydrophilic residues also exist in the interior active site to stabilize hydrophilic portions of the substrate during catalysis.