TY - JOUR
T1 - A CURE Biochemistry Laboratory Module to Study Protein-Protein Interactions by NMR Spectroscopy
AU - Marsiglia, William M.
AU - Qamra, Rohini
AU - Jackson, Kimberly M.
AU - Traaseth, Nathaniel J.
N1 - Funding Information:
This work was supported by the National Science Foundation (MCB1506420) (to N.J.T). The NMR data collected at NYU were collected on a cryogenic probe made available by funding from the National Institutes of Health (S10OD016343). W.M.M. acknowledges predoctoral funding from the National Institutes of Health (F99CA212474). We are grateful to Moosa Mohammadi for generously providing the plasmid for expressing the SH2 domain and to Shanina Sanders Johnson for providing NMR support at Spelman College.
Publisher Copyright:
Copyright © 2020 American Chemical Society and Division of Chemical Education, Inc.
PY - 2020/2/11
Y1 - 2020/2/11
N2 - The design of undergraduate laboratory courses that provide meaningful research-based experiences enhances undergraduate curricula and prepares future graduate students for research careers. In this article, a course-based undergraduate research experience (CURE) laboratory module was designed for upper-division undergraduate biochemistry and chemistry students. The laboratory module enabled students to build upon recently published data in the literature to decipher atomistic insight for an essential protein-protein interaction in human biology through the use of biomolecular NMR spectroscopy. Students compared their results with published data with the goal of identifying specific regions of the protein-protein interaction responsible for triggering an allosteric conformational change. The laboratory module introduced students to basic and advanced laboratory techniques, including protein purification, NMR spectroscopy, and analysis of protein structure using molecular visualization software.
AB - The design of undergraduate laboratory courses that provide meaningful research-based experiences enhances undergraduate curricula and prepares future graduate students for research careers. In this article, a course-based undergraduate research experience (CURE) laboratory module was designed for upper-division undergraduate biochemistry and chemistry students. The laboratory module enabled students to build upon recently published data in the literature to decipher atomistic insight for an essential protein-protein interaction in human biology through the use of biomolecular NMR spectroscopy. Students compared their results with published data with the goal of identifying specific regions of the protein-protein interaction responsible for triggering an allosteric conformational change. The laboratory module introduced students to basic and advanced laboratory techniques, including protein purification, NMR spectroscopy, and analysis of protein structure using molecular visualization software.
KW - Biochemistry
KW - Biophysical Chemistry
KW - Inquiry-Based/Discovery Learning
KW - NMR Spectroscopy
KW - Proteins/Peptides
KW - Upper-Division Undergraduate
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U2 - 10.1021/acs.jchemed.9b00364
DO - 10.1021/acs.jchemed.9b00364
M3 - Article
AN - SCOPUS:85078741334
SN - 0021-9584
VL - 97
SP - 437
EP - 442
JO - Journal of Chemical Education
JF - Journal of Chemical Education
IS - 2
ER -