User:Adriana Kita/Sandbox 1
From Proteopedia
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| - | + | == Human beta-glucocerebrosidase == | |
| - | Description of GCB goes here. | ||
| - | I can describe more about GCB here. | ||
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| - | <scene name='User:Adriana_Kita/Sandbox_1/Gcase_disulfide_1/1'>View of disulfide bonds</scene> | ||
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{{Clear}} | {{Clear}} | ||
<applet load='1ogs' size='[450,338]' frame='true' align='right' | <applet load='1ogs' size='[450,338]' frame='true' align='right' | ||
| - | caption=' | + | caption='Human beta-glucocerebrosidase (1ogs)' scene='User:Adriana_Kita/Sandbox_1/Gcase_whole/5'/> |
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| + | Human beta-glucocerebrosidase, also known as glucoceremidase, GCase, and velaglucerase, is an enzyme that is commonly found to be deficient in patients with Gaucher's disease. | ||
| + | Currently, there are two drugs on the market to treat this disease. One being Genzyme's Cerezyme and the other SHIRE's VPRIV. | ||
| + | |||
| + | The typical method used to sequence current biologics, as well as map post translational modifications, is a combination of proteolytic digestion followed by LC/MS. Unfortunately, sometimes this method is not enough for complete identification of some post translational modifications. I am interested in the oxidation of Cys residues for the formation of disulfide bonds. | ||
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| + | {{Clear}} | ||
| + | <applet load='1ogs' size='[450,338]' frame='true' align='right' | ||
| + | caption='Disulfide Connectivity of GCase' scene='User:Adriana_Kita/Sandbox_1/Gcase_disulfide_1/2'/> | ||
=== Disulfide Structure === | === Disulfide Structure === | ||
| + | Human beta-glucocerebrosidase (GCase) has seven Cys residues, four of which make two disulfide bonds. These two disufide bonds are both located in the N-terminal region of the protein and separated by only one amino acid. One of my current projects is using mass spectrometry to discern the disulfide connectivity in regions of a protein that are rich with Cys residues. | ||
| - | The spinning protein (<scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'>Initial view</scene>) ) is human beta-glucosidase. | ||
| - | Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/ | ||
| + | '''GCase N-terminal residues 1-23:''' ''ARPCIPKSFGYSSVVCVCNATYCDS'' | ||
| - | + | '''Disulfide Connectivity:''' ''C4-C16 & C18-C23'' | |
Current revision
Human beta-glucocerebrosidase
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Human beta-glucocerebrosidase, also known as glucoceremidase, GCase, and velaglucerase, is an enzyme that is commonly found to be deficient in patients with Gaucher's disease.
Currently, there are two drugs on the market to treat this disease. One being Genzyme's Cerezyme and the other SHIRE's VPRIV.
The typical method used to sequence current biologics, as well as map post translational modifications, is a combination of proteolytic digestion followed by LC/MS. Unfortunately, sometimes this method is not enough for complete identification of some post translational modifications. I am interested in the oxidation of Cys residues for the formation of disulfide bonds.
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Disulfide Structure
Human beta-glucocerebrosidase (GCase) has seven Cys residues, four of which make two disulfide bonds. These two disufide bonds are both located in the N-terminal region of the protein and separated by only one amino acid. One of my current projects is using mass spectrometry to discern the disulfide connectivity in regions of a protein that are rich with Cys residues.
GCase N-terminal residues 1-23: ARPCIPKSFGYSSVVCVCNATYCDS
Disulfide Connectivity: C4-C16 & C18-C23
