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NMR Titration Used to Observe Specific Proton Dissociation in Polyprotic Tripeptides: An Undergraduate Biochemistry Lab

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J. L. Yarger , R. A. Nieman and A. L. Bieber

Arizona State University, Tempe, AZ 85287

J. Chem. Educ., 1997, 74 (2), p 243

DOI: 10.1021/ed074p243

Publication Date (Web): February 1, 1997

Section:

History, Education, and Documentation

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.

Keywords (Audience):

Upper-Division Undergraduate

Keywords (Domain):

Biochemistry

Keywords (Pedagogy):

Hands-On Learning / Manipulatives

Keywords (Subject):

NMR Spectroscopy

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This article has been cited by 2 ACS Journal articles (2 most recent appear below).

Spin Coherence Transfer in Chemical Transformations Monitored by Remote Detection NMR
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Analytical Chemistry2007 79 (7), 2806-2811
- Spin Coherence Transfer in Chemical Transformations Monitored by Remote Detection NMR
  M. Sabieh Anwar, Christian Hilty, Chester Chu, Louis-S. Bouchard, Kimberly L. Pierce, and Alexander Pines
  Analytical Chemistry2007 79 (7), 2806-2811
  We demonstrate a nuclear magnetic resonance (NMR) experiment using continuous flow in a microfluidic channel for studying the transfer of spin coherence in nonequilibrium chemical processes. We use the principle of remote detection, which involves ...
  Abstract | Full Text HTML | Hi-Res PDF
Using Infrared Spectroscopy to Investigate Protein Structure
Janet Olchowicz , Deidra R. Coles , Lori E. Kain and Gina MacDonald
Journal of Chemical Education2002 79 (3), 369
- Using Infrared Spectroscopy to Investigate Protein Structure
  Janet Olchowicz , Deidra R. Coles , Lori E. Kain and Gina MacDonald
  Journal of Chemical Education2002 79 (3), 369
  This report describes a laboratory that employs infrared spectroscopy to observe protein secondary structure. The techniques utilized are suitable for all levels of biochemistry or biophysical chemistry laboratories. Students first obtain absorbance ...
  Abstract | Hi-Res PDF | PDF w/ Links