Elizeu/sandbox/citocromo c
From Proteopedia
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== Introduction == | == Introduction == | ||
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' /> | <Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' /> | ||
| - | Haemoglobin 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 | + | Haemoglobin 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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== Exploring the Structure == | == Exploring the Structure == | ||
| + | Haemoglobin (Hb) consists of 2 identical &alpha subunits and 2 identical &beta subunits. The strongest inter-subunit interactions exist between the &alpha and &beta subunits so Hb could be considered to be a dimer of &alpha/&beta subunits. The &alpha subunits have 141 residues while &beta subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O<sub>2</sub> coordination. | ||
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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]] | [[Image:oxyHb.png]] | ||
Revision as of 22:54, 21 January 2015
The Structure Function Relationship of Haemoglobin
Introduction
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Haemoglobin 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 O2 to be picked up in the lungs and delivered to the tissues.
Exploring the Structure
Haemoglobin (Hb) consists of 2 identical &alpha subunits and 2 identical &beta subunits. The strongest inter-subunit interactions exist between the &alpha and &beta subunits so Hb could be considered to be a dimer of &alpha/&beta subunits. The &alpha subunits have 141 residues while &beta subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.
On the right is . 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.
Proteopedia Page Contributors and Editors (what is this?)
Julie Langlois, Atena Farhangian, Rebecca Holstein, Elizabeth A. Dunlap, Katherine Reynolds, Elizeu Santos, Noam Gonen, Anna Lohning, Idan Ben-Nachum, Brian Ochoa, Shai Biran, Gauri Misra, Shira Weingarten-Gabbay, Keni Vidilaseris, Jamie Costa, Abhinav Mittal, Urs Leisinger, Madison Walberry, Edmond R Atalla, Brett M. Thumm, Brooke Fenn, Joel L. Sussman, Mati Cohen, Vesta Nwankwo, Dotan Shaniv, Gulalai Shah
