Sandbox 46: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Student (talk | contribs)
No edit summary
Student (talk | contribs)
No edit summary
Line 4: Line 4:
<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Sandbox_46/1ake_main/2' />
<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Sandbox_46/1ake_main/2' />
=Adenylate Kinase=
=Adenylate Kinase=
Adenylate Kinase is a enzyme that catalyzes the conversion of 2 units of ADP into a unit of ATP and a unit of AMP. It is because of this catalytic role that adenylate kinase is an important part of homeostasis.
<scene name='Sandbox_46/1ake_main/2'>Adenylate kinase</scene>  is a enzyme that catalyzes the conversion of 2 units of ADP into a unit of ATP and a unit of AMP. It is because of this catalytic role that adenylate kinase is an important part of homeostasis.
=Structure=
=Structure=
<scene name='Sandbox_46/1ake_main/2'>Chain A</scene>


The <scene name='Sandbox_46/1ake_secondary/1'>secondary structure</scene> of adenylate kinase shows alpha helices (blue) and beta sheets (teal) surrounding the non-hydrolysable substrate analogue.
The <scene name='Sandbox_46/1ake_secondary/1'>secondary structure</scene> of adenylate kinase shows alpha helices (blue) and beta sheets (teal) surrounding the non-hydrolysable substrate analogue. The enzyme is comprised of 9 helices and 9 sheets constituting the secondary structure. As with any enzyme, the <scene name='Sandbox_46/1ake_hydrogen/1'>hydrogen bonds</scene> between the residues of the peptide chains supply the final folded protein with structural stability to remain folded.
 
<scene name='Sandbox_46/1ake_hydrogen/1'>Hydrogen Bonds</scene>


The <scene name='Sandbox_46/1ake_phobicphilic/2'>hydrophobic and hydrophilic residues</scene> are represented in grey and purple respectively.
The <scene name='Sandbox_46/1ake_phobicphilic/2'>hydrophobic and hydrophilic residues</scene> are represented in grey and purple respectively.