Sandbox 34: Difference between revisions

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However, the hydrophobic interactions are not the only thing holding it together or helping to keep its conformation. There are also many <scene name='Sandbox_34/Adenylate_kinase_andpolarside/1'>polar and charged side groups (green)</scene> that help maintain the hydrophobic interactions and help stabilize the protein by interacting with one another. The interaction between the polar groups and the hydrophobic groups can be seen by the pink transparent hydrophobic groups and the green polar groups.

Proteins can be crystallized which can be very helpful for understanding the relative shape and sometimes functions of the protein. When proteins are crystallized they often have water molecules embedded in them because of how tightly and deep the water molecules can become wedged in the protein. The <scene name='Sandbox_34/Adenylate_kinase_water/1'>water molecule interactions (magenta)</scene> with the protein can be seen surrounding and inside some parts of the protein.

Proteins can be crystallized which can be very helpful for understanding the relative shape and sometimes functions of the protein. When proteins are crystallized they often have water molecules embedded in them because of how tightly and deep the water molecules can become wedged in the protein. The <scene name='Sandbox_34/Adenylate_kinase_water/1'>water molecule interactions (magenta)</scene> with the protein can be seen surrounding and inside some parts of the protein. The parts of the protein that are interacting with the water molecules are hydrophilic and the parts not interacting with the water molecules are hydrophobic.

Sandbox 34: Difference between revisions

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Revision as of 00:37, 18 October 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 00:41, 18 October 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	However, the hydrophobic interactions are not the only thing holding it together or helping to keep its conformation. There are also many <scene name='Sandbox_34/Adenylate_kinase_andpolarside/1'>polar and charged side groups (green)</scene> that help maintain the hydrophobic interactions and help stabilize the protein by interacting with one another. The interaction between the polar groups and the hydrophobic groups can be seen by the pink transparent hydrophobic groups and the green polar groups.		However, the hydrophobic interactions are not the only thing holding it together or helping to keep its conformation. There are also many <scene name='Sandbox_34/Adenylate_kinase_andpolarside/1'>polar and charged side groups (green)</scene> that help maintain the hydrophobic interactions and help stabilize the protein by interacting with one another. The interaction between the polar groups and the hydrophobic groups can be seen by the pink transparent hydrophobic groups and the green polar groups.

	Proteins can be crystallized which can be very helpful for understanding the relative shape and sometimes functions of the protein. When proteins are crystallized they often have water molecules embedded in them because of how tightly and deep the water molecules can become wedged in the protein. The <scene name='Sandbox_34/Adenylate_kinase_water/1'>water molecule interactions (magenta)</scene> with the protein can be seen surrounding and inside some parts of the protein.		Proteins can be crystallized which can be very helpful for understanding the relative shape and sometimes functions of the protein. When proteins are crystallized they often have water molecules embedded in them because of how tightly and deep the water molecules can become wedged in the protein. The <scene name='Sandbox_34/Adenylate_kinase_water/1'>water molecule interactions (magenta)</scene> with the protein can be seen surrounding and inside some parts of the protein. The parts of the protein that are interacting with the water molecules are hydrophilic and the parts not interacting with the water molecules are hydrophobic.