Elizeu/sandbox/citocromo c

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==The Structure Function Relationship of Haemoglobin==
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== Example page for Green fluorescent protein ("GFP") ==
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<StructureSection load='1ema' size='300' frame='true' side='right' caption='GFP ([[1ema]])' scene=''>
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[[Image:1ema.gif|thumb|left|450px|Green fluorescent protein (1ema)]]
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== Introduction ==
== Introduction ==
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<Structure load='1hho_mm1.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='OxyHb' />
 
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<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O<sub>2</sub> to be picked up in the lungs and delivered to the tissues.
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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.
== Exploring the Structure ==
== Exploring the Structure ==
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Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O<sub>2</sub> coordination.
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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
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<scene name='Sandbox_4/Green_fp/1'>chromophore</scene>, 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.<ref>PMID:8703075</ref>
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On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.
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[[Image:oxyHb.png]]
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</StructureSection>
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The key to Hb's success is conformational changes which increase or decrease its affinity for O<sub>2</sub>. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
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==References==
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What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO<sub>2</sub> and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O<sub>2</sub> binding site and effect a change in conformation of Hb.
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<references/>

Revision as of 07:31, 17 April 2015

Example page for Green fluorescent protein ("GFP")

GFP (1ema)

Drag the structure with the mouse to rotate

References

  1. ↑ Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075
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