Elizeu/sandbox/citocromo c
From Proteopedia
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==The Structure Function Relationship of Haemoglobin== | ==The Structure Function Relationship of Haemoglobin== | ||
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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 oxygen to be picked up in the lungs and delivered to the tissues. | 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 oxygen to be picked up in the lungs and delivered to the tissues. | ||
| - | + | This is oxyhaemoglobin. 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. | |
| + | <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene> | ||
== Exploring the Structure == | == Exploring the Structure == | ||
[[Image:oxyHb.png]] | [[Image:oxyHb.png]] | ||
Revision as of 09:06, 21 January 2015
The Structure Function Relationship of Haemoglobin
Introduction
|
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 oxygen to be picked up in the lungs and delivered to the tissues. This is oxyhaemoglobin. 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.
Exploring the Structure
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
