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  Home > JCE Print > Journal of Chemical Education > Issues > 1997  > February  >
In the Laboratory
NMR Titration Used to Observe Specific Proton Dissociation in Polyprotic Tripeptides: An Undergraduate Biochemistry Lab
J. L. Yarger, R. A. Nieman, and A. L. Bieber
Arizona State University, Tempe, AZ 85287
Cover
February 1997
Vol. 74 No. 2
p. 243
Abstract
NMR can provide a wealth of information on the dynamic processes of proteins in their natural aqueous environment and is the only technique that can determine polypeptide or protein structure in solution. The procedures and strategies that are common today for studying structure and dynamics of biological systems have been developed in the course of the last twenty years (2). Despite the establishment of NMR in biochemical research, this technique has not been incorporated into many biochemistry laboratory courses. The paucity of advanced biochemistry laboratory experiments motivated us to create this experiment, which illustrates basic 1- and 2-D NMR techniques used to study specific proton dissociation in peptides.
More Information
*  Citation
 Yarger, J. L.; Nieman, R. A.; Bieber, A. L. . J. Chem. Educ. 1997 74 243.
*  Keywords
*  History
 Created:
Last Updated:		 July 29, 1999
June 23, 2005
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