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Myoglobin
KSU Stark   Clarke Earley

Myoglobin

Myoglobin is a commonly illustrated example of a biologically important protein. The primary role of myoglobin is for storage of oxygen. The structure below is the deoxygenated form of sperm whale myoglobin, taken from the Brookhaven Protein Database (structure ref = 5MBN, author = T. Takano).

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


Solvent
Off
Ball & Stick

Iron Heme
Off
Wireframe
Ball & Stick
Spacefilling


Combinations
Near Fe (5.0 A)
Show Fe & N
Heme & Histidine


Lighting
100%
75%
60%
40%

Levels of structure in Myoglobin

Primary structure
The sequence of amino acids in the single polypeptide chain of this molecule.
Secondary structure
The three-dimensional arrangement of the protein backbone. Best illustrated in this drawing by selecting "Backbone", "Ribbons", or "Ribbons +". In this molecule, the alpha helices are clearly seen.
Tertiary structure
The three-dimensional arrangement of the protein, including all side chains. The "Wireframe" and "Ball & Stick" views give the best illustration of this structure level.
Quaternary structure
Focuses on interaction of different polypeptide chains. This can be best illustrated by examination of the Hemoglobin stucture, which consists of four polypeptide chains, each of which is similar to myoglobin.

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: Wed Nov 11 15:34:53 1998 GMT
Page accessed 1934 times since Wed Apr 28 16:12:09 1999 GMT