Proteopedia - User contributions [en]

File:E1f5a122-2946-11e4-91d8-005056020102.pdb

2014-08-21T15:39:19Z

Abhinav Mittal:

File:12.pdb

2014-08-20T18:10:46Z

Abhinav Mittal:

Elizeu/sandbox/citocromo c

2014-08-20T18:09:16Z

Abhinav Mittal:

== Exploring the structure ==
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.
Exploring the Structure

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 '''<scene name='Sandbox_3/1ema/1'>chromophore</scene>''' 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.[1]
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' with caption='GFP (PDB entry [[1ema]])</StructureSection>

Elizeu/sandbox/citocromo c

2014-08-20T17:45:42Z

Abhinav Mittal:

<Structure load='3r8s' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />== Exploring the structure ==
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.
Exploring the Structure

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 '''<scene name='Sandbox_3/1ema/1'>chromophore</scene>''' 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.[1]
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' with caption='GFP (PDB entry [[1ema]])</StructureSection>