Sandbox reserve 103

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<Structure load='3omv' size='500' frame='true' align='right' caption='C-Raf'
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>One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the Peyton group and on display at the [http://www.molecularplayground.org Molecular Playground].
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Protein Database (PDBsum): 3omv. European Bioinformatics (EBI); 2009.</ref> GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light.<ref name="Yang">[http://www-bioc.rice.edu/Bioch/Phillips/Papers/gfpbio.html], Yang F, Moss LG, Phillips GN Jr. 1996. The molecular structure of green fluorescent protein. Biotechnology. 14: 1246-1251. DOI 10.1038/nbt1096-1246.</ref> It remains unclear why these jellyfish use fluorescence, why green is better than blue, or why they produce a separate protein for green fluorescence as opposed to simply mutating the present aequorin to shift its wavelength,<ref name="Tsien" /> but in the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others.<ref name="Haldar">[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A. 2009. The green journey. J Fluoresc. 19:1-2. DOI 10.1007/s10895-008-0455-6; biographical background on [http://en.wikipedia.org/wiki/Douglas_Prasher Douglas Prasher], [http://en.wikipedia.org/wiki/Martin_Chalfie Martin Chalfie] and [http://en.wikipedia.org/wiki/Roger_Tsien Roger Tsien].</ref>
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<StructureSection load='3omv' size='500' side='right' scene='User:Thuy V. Nguyen/sandbox103/C-Raf' caption='C-Raf'>
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'''Insulin''' is a hormone that controls [[Carbohydrate Metabolism|carbohydrate 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. Proinsulin (Pins) is processed by several proteases in the Golgi apparatus to form insulin which is shorter by 35 amino acids. DPI is a monomeric despentapeptide (B26-B30) Ins analogue. DTRI is a monomeric destripeptide (B28-B30) Ins analogue. DHPI is for desheptapeptide (B24-B30) Ins. LIns is a legume Ins.
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==References==
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&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;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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{{Reflist}}
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&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains. These <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>hydrogen bonds</scene> 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 <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4'>hexameric form</scene> in the body. This <scene name='User:Whitney_Stoppel/sandbox1/Insulin_ph7/2'>scene highlights</scene> 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_Drugs#Treatments|pharmaceutical use]].
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</StructureSection>
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==Additional Resources==
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*For additional information, see: [[Colored & Bioluminescent Proteins]]
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*[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ema First Glance]
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*PDBsum: [http://www.ebi.ac.uk/pdbsum/1ema 1ema]
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*RCSB PDB [http://www.rcsb.org/pdb/explore.do?structureId=1ema 1ema]
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*[http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ema OCA]
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*UniProt: [http://www.uniprot.org/uniprot/P42212 P42212]
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*Scop: [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.e.gc.b.b.b.html P42212]
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*CATH: [http://www.cathdb.info/domain/1emaA00 1emaA00]
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*Pfam: [http://pfam.sanger.ac.uk/family?acc=PF01353 PF01353]
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*InterPro: [http://www.ebi.ac.uk/interpro/ISearch?query=IPR000786 IPR000786]
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*[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb42_1.html GFP featured] at the '''[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]''' series of tutorials by [[User:David_S._Goodsell|David Goodsell]].
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* [http://www.nature.com/nature/journal/v462/n7270/edsumm/e091112-05.html Inside green fluorescent protein] - editor's summary that accompanied [http://www.nature.com/nature/journal/v462/n7270/covers/ structural detail of GFP chromophore on the cover] of Nature.
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[[he:GFP_(Hebrew)]]
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[[Category:Topic Page]]
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Revision as of 19:05, 16 December 2011

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

C-Raf

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