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Hemoglobin




KSU Stark   Clarke Earley

Hemoglobin

Hemoglobin is a commonly illustrated example of a biologically important protein. The primary role of hemoglobin is for transport of oxygen. The structure below is the deoxygenated form of hemoglobin from a Antartic fish, taken from the Brookhaven Protein Database (structure ref = 1HBH, authors = N. Ito, N.H. Komiyama, and G. Fermi).

In order to view this molecule correctly, you must have the CHIME Plug-in properly installed. To rotate this molecule, move your pointer over the structure, then hold the button down while 'dragging' the pointer.


Protein
Off
Wireframe
Ball & Stick
Spacefilling
Backbone
Ribbons
Ribbons +
Polar
Hydrophobic
Quaternary Balls
Quaternary Space
Quaternary Ribbon


Solvent
Off
Ball & Stick
Iron Heme
Off
Wireframe
Ball & Stick
Spacefilling
Near Fe (5.0 A)
 
 
Lighting
100%
75%
60%
40%

Quaternary structure

Hemoglobin is a classic example of a molecule that illustrates quaternary structure. This compound contains four separate polypeptide chains that are held fairly tightly together by a large number of intermolecular forces. While these four chains cannot easily be seen in any of the protein views, selecting "Quaternary Balls" or "Quaternary Space" provides diagrams where each of the chains is colored differently.


Fall 1997ResearchServiceComputer Circle
OrganicOrganic LaboratoryPhysiological Chemistry


This page was last modified on September 01, 1997
and was written and is maintained by
Clarke Earley
Kent State University Stark Campus
Department of Chemistry
email:
cearley@stark.kent.edu
© 1997 by Clarke Earley, Kent State University.

Modified: Tue Sep 30 16:00:00 1997 GMT
Page accessed 1482 times since Mon Jan 29 12:57:47 2001 GMT