User:Whitney Stoppel/sandbox1

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<applet size='[450,338]' frame='true' align='right'
<applet size='[450,338]' frame='true' align='right'
caption='Insulin, showing disulfide bridges between the A-chain and B-chain' /> <scene name='User:Whitney_Stoppel/sandbox1/Human_insulin2/1'>Insulin</scene>
caption='Insulin, showing disulfide bridges between the A-chain and B-chain' /> <scene name='User:Whitney_Stoppel/sandbox1/Human_insulin2/1'>Insulin</scene>
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Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively. These two chains are joined by disulfide bonds, which are shown in yellow. This single piece made up of the A- and B-chains is the active form of the insulin hormone. This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively. These two chains are joined by disulfide bonds, which are shown in yellow. This single piece made up of the A- and B-chains is the active form of the insulin hormone. This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.
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<applet size='[450,338]' frame='true' align='right'
<applet size='[450,338]' frame='true' align='right'
caption='Insulin dimer, with hydrogen bonding shown in white' /> <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>Hydrogen Bonding in an Insulin Dimer</scene>
caption='Insulin dimer, with hydrogen bonding shown in white' /> <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>Hydrogen Bonding in an Insulin Dimer</scene>
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Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains. These hydrogen bonds are shown above in white. Then, 3 dimers can come together in the presence of zinc ions and form a hexamer. Insulin is stored in the hexameric form in the body.
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains. These hydrogen bonds are shown above in white. Then, 3 dimers can come together in the presence of zinc ions and form a hexamer. Insulin is stored in the hexameric form in the body.
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<applet size='[450,338]' frame='true' align='right'
<applet size='[450,338]' frame='true' align='right'
caption='Symmetric insulin hexamer with zinc ions shown' /> <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3'>Symmetric Insulin Hexamer</scene>
caption='Symmetric insulin hexamer with zinc ions shown' /> <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3'>Symmetric Insulin Hexamer</scene>
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Insulin is a hormone that controls sugar metabolism and storage in the human body. The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas. Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes. The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.
Insulin is a hormone that controls sugar metabolism and storage in the human body. The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas. Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes. The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.

Revision as of 14:17, 30 April 2010

One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst in the Roberts Research Group and on display at the Molecular Playground.

Insulin, showing disulfide bridges between the A-chain and B-chain

Drag the structure with the mouse to rotate




Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively. These two chains are joined by disulfide bonds, which are shown in yellow. This single piece made up of the A- and B-chains is the active form of the insulin hormone. This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.

Insulin dimer, with hydrogen bonding shown in white

Drag the structure with the mouse to rotate






Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains. These hydrogen bonds are shown above in white. Then, 3 dimers can come together in the presence of zinc ions and form a hexamer. Insulin is stored in the hexameric form in the body.

Symmetric insulin hexamer with zinc ions shown

Drag the structure with the mouse to rotate





Insulin is a hormone that controls sugar metabolism and storage in the human body. The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas. Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes. The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.

Insulin monomer at pH 7 with hydrophobic sections shown in gray

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Whitney Stoppel

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