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| | ==Your Heading Here (maybe something like 'Structure')== |
| | <StructureSection load='5eqh' size='350' side='right' caption='GLUT1 transporter in complex with inhibitor (PDB entry [[5eqh]])' scene=''> |
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| Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
| | Anything in this section will appear adjacent to the 3D structure and will be scrollable. |
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| | <scene name='10/101618/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45 |
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| == Exploring the Structure ==
| | </StructureSection> |
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| GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.
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