Sandbox 40
From Proteopedia
| Line 15: | Line 15: | ||
<scene name='Sandbox_40/Vine_veiw_of_disulfide_bonds/1'>Cysteines </scene> | <scene name='Sandbox_40/Vine_veiw_of_disulfide_bonds/1'>Cysteines </scene> | ||
| - | As it is in all proteins, | + | As it is in all proteins, the hydrophobic effect is the strongest force that holds lysozyme's three-dimensional structure in place. In the following view, the hydrophilic residues are shown in purple and the hydrophobic residues are shown in gray. |
| - | <scene name='Sandbox_40/Hydrophobic_interaction/1'> | + | <scene name='Sandbox_40/Hydrophobic_interaction/1'>Hydrophobic View</scene> |
| + | |||
| + | This view focuses on the hydrophobic interactions of one helix of the enzyme. | ||
Revision as of 21:54, 29 October 2010
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
|
LYSOZYME
Lysozyme is an enzyme found in the secretions and tissues of most animals. It destroys bacterial cell walls by hydrolysing the glycosidic linkages in cell wall peptidoglycans.
The enzyme's tertiary structure is maintained in part by disulfide bonds. the following view displays the enzyme from residue number 60 to 102. it shows two disulfide bonds stabilizing two alpha helices and the loop connecting them.
This scene shows the same group of residues with the four cysteines responsible for the the disulfide bonds highlighted with yellow halos.
As it is in all proteins, the hydrophobic effect is the strongest force that holds lysozyme's three-dimensional structure in place. In the following view, the hydrophilic residues are shown in purple and the hydrophobic residues are shown in gray.
This view focuses on the hydrophobic interactions of one helix of the enzyme.
