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  Home > JCE Print > Journal of Chemical Education > Issues > 1998  > December  >
In the Laboratory
Concepts in Biochemistry
A Thermodynamic Study of Azide Binding to Myoglobin
Anne T. Marcoline and Timothy E. Elgren
Hamilton College, Department of Chemistry, 198 College Hill Road, Clinton, NY 13323
Cover
December 1998
Vol. 75 No. 12
p. 1622
Abstract
The visible absorption spectrum associated with the heme protein myoglobin changes as a result of azide binding to the iron center. Therefore, a titration with azide can be monitored and concentrations of the myoglobin-azide adduct quantified. From these ligand binding data, the dissociation constant and number of binding sites can be determined using the Scatchard method for analysis. This laboratory project can be completed in two 3-hour lab periods. Evaluation of other thermodynamic properties is possible by exploring the temperature dependence of these binding data. A third lab period is required for students to probe the temperature dependence.
Supplement
The laboratory experiment is a Microsoft Word document for Macintosh and has been compressed into a sit (for Macintosh) and a zip (for Windows) file. This detailed version of the experiment can also be accessed as a pdf file using Acrobat Reader.
*  Contents
*  Download
supp1622.pdf

supp1622.sit

supp1622.zip
More Information
*  Citation
 Marcoline, Anne T.; Elgren, Timothy E. J. Chem. Educ. 1998 75 1622.
*  Keywords
 Thermodynamics; UV-Vis Spectroscopy; Proteins / Peptides; Biochemistry; Bioinorganic Chemistry; Laboratory Instruction
*  History
 Created:
Last Updated:		 June 18, 1999
November 22, 2005
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