Sandbox Reserved 794
From Proteopedia
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- | The <scene name='56/563206/Pgk_hydrophobicres/2'>hydrophobic residues</scene> are showed in grey. Hydrophobic residues are usually found inside the protein since they dislike water interactions. The <scene name='56/563206/Pgk_hydrophilicresi/1'>hydrophilic residues</scene> | + | The <scene name='56/563206/Pgk_hydrophobicres/2'>hydrophobic residues</scene> are showed in grey. Hydrophobic residues are usually found inside the protein since they dislike water interactions. The <scene name='56/563206/Pgk_hydrophilicresi/1'>hydrophilic residues</scene> are shown in red. The hydrophilic residues are usually found on the outside of the protein since they prefer water interactions over hydrophobic residues. |
Revision as of 23:58, 8 October 2013
This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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The of phosphoglycerate kinase shows alpha helices (purple) and beta sheets (green).
Phosphoglycerate kinase's are shown in orange. Majority of the hydrogen bonds are parallel. One can see the parallel hydrogen bonds by observing the alpha helices and beta sheets. The parallel conformation leads to a diagonal bond where as the antiparallel conformation leads to more straight up and down bonds. Disulfide bonds are not present in phosphoglycerate kinase.
The are showed in grey. Hydrophobic residues are usually found inside the protein since they dislike water interactions. The are shown in red. The hydrophilic residues are usually found on the outside of the protein since they prefer water interactions over hydrophobic residues.