Hoelzer Sandbox: Difference between revisions
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Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. | Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. | ||
To design our model of the β2-adrenergic receptor, we used the atomic coordinates for this structure as reported in the <scene name='Hoelzer_Sandbox/Spacefilled/1'>pdb file 2rh1</scene>, from the Ray Stevens laboratory at the Scripps Research Institute. Our model represents <scene name='Hoelzer_Sandbox/Spacefilled_1/1'>amino acids 29-230 and 263-342 </scene>. Starting with a cpk-colored, spacefilled representation of the protein, we simplified this image by converting it to an <scene name='Hoelzer_Sandbox/Spacefilled_3/1'>alpha-carbon backbone representation</scene>. We colored the seven trans-membrane alpha helices green --- connected by loops that we colored gray. We then displayed four sidechains <scene name='Hoelzer_Sandbox/Spacefilled_4/2'>(Phe 193, Trp 286, Phe 289, and Phe 290)</scene> involved in the binding of a beta-blocker, and colored them blue. The beta-blocker, Carazolol, was then added in a ball-and-stick format, colored orange. The three cholesterol molecules resolved in this structure, bound to the outside surface of the protein, were added and displayed in a ball-and-stick format, colored red. Finally, the N-terminal end of the protein was colored blue, and the C-terminal end was colored magenta. | To design our model of the β2-adrenergic receptor, we used the atomic coordinates for this structure as reported in the <scene name='Hoelzer_Sandbox/Spacefilled/1'>pdb file 2rh1</scene>, from the Ray Stevens laboratory at the Scripps Research Institute. Our model represents <scene name='Hoelzer_Sandbox/Spacefilled_1/1'>amino acids 29-230 and 263-342 </scene>. Starting with a cpk-colored, spacefilled representation of the protein, we simplified this image by converting it to an <scene name='Hoelzer_Sandbox/Spacefilled_3/1'>alpha-carbon backbone representation</scene>. We colored the seven trans-membrane alpha helices green --- connected by loops that we colored gray. We then displayed four sidechains <scene name='Hoelzer_Sandbox/Spacefilled_4/2'>(Phe 193, Trp 286, Phe 289, and Phe 290)</scene> involved in the binding of a beta-blocker, and colored them blue. The beta-blocker, <scene name='Hoelzer_Sandbox/Spacefilled_4/4'>Carazolol</scene>, was then added in a ball-and-stick format, colored orange. The three cholesterol molecules resolved in this structure, bound to the outside surface of the protein, were added and displayed in a ball-and-stick format, colored red. Finally, the N-terminal end of the protein was colored blue, and the C-terminal end was colored magenta. | ||
A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer. | A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer. |