NMSU - Department of Chemisty and Biochemistry

BARBARA A. LYONS

Associate Professor

B.S., California Polytechnic State University

at San Luis Obispo 1983
M.S., Cornell University, New York 1985
Ph.D., Cornell University, New York 1989
Postdoctoral, Rutgers University,

Piscataway, New Jersey 1990-1993
Postdoctoral, Schering Plough Research Institute,

Kenilworth, New Jersey 1993-1995

blyons@nmsu.edu
(575) 646-6702

RESEARCH PUBLICATIONS COURSE LINKS

Our laboratory is interested in determining the three-dimensional structures of small proteins in solution by multidimensional multinuclear nuclear magnetic resonance (NMR) spectroscopy. Current projects underway in the laboratory focus on relating structure to function and specificity in the Grb7 protein family. Members of this protein family have all been implicated in an increased occurrence of cancer. Specifically, Grb7 expression is up-regulated in 20-30% of breast cancers and these patients have a poor long-term survival rate. Our research is focused on unraveling the structural basis for the propensity of this protein family to bind only to specific up-stream and down-stream signaling partners. Study in this field spans a wide breadth of experimental approaches, including molecular biology, expression, and purification of proteins of interest, knowledge and implementation of data acquisition techniques using the NMR spectrometer, extensive data analysis and interpretation using available software on Unix based computers, and calculation and refinement of three-dimensional structures derived from NOE distance constraints.

RECENT PUBLICATIONS:

Solution Structure of the Grb14-SH2 Domain and Comparison to the Structure and Backbone Relaxation Behavior of the Grb7-SH2/erbB2 Peptide Complex.
Scharf, P.J.; Ivancic, M.; Guth, E.C.; Witney, J.; Daugherty, M.A.; Lyons, B.A.
(Submitted to: Proteins: Structure, Function, and Bioinformatics)
Solution Structure of the Human Grb7-SH2 Domain/erbB2 Peptide Complex and Structural Basis for Grb7 Binding to erbB2.
Ivancic, M.; Daly, R.J.; Lyons, B.A. (2003)
J Biomol NMR, Nov;27(3):205-19.
Assignment of Backbone 1H, 13C, and 15N Resonances of the SH2 Domain of Human Grb14.
Scharf, P.J.; Lyons B.A. (2002)
J Biomol NMR, Nov;24(3):275-6.
Assignment of Backbone 1H, 13C, and 15N Resonances of Human Grb7-SH2 Domain in Complex with a Phosphorylated Peptide Ligand.
Brescia, P.J.; Ivancic, M.; Lyons, B.A. (2002)
J Biomol NMR, May;23(1):77-8.
Spectral and Metal-Binding Properties of Three Single-Point Tryptophan Mutants of Human Transferrin N-Lobe.
He, Q.Y.; Mason, A.; Lyons, B.; Tam, B.; Nguyen, V.; MacGillivray, R.; Woodworth, R. (2001)
The Biochemistry Journal 354, 423.
Uracil Glycol Deoxynucleoside Triphosphate is a Better Substrate for DNA Polymerase I Klenow Fragment than Thymine Glycol Deoxynucleoside Triphosphate.
Purmal, A.A.; Bond, J.P.; Lyons, B.A.; Kow, Y.W.; & Wallace, S.S. (1998)
Biochemistry 37(1):330-8.
Chemical Shift Assignments and Secondary Structure of the Grb2 SH2 Domain by Heteronuclear NMR Spectroscopy.
Wang, Y.S.; Frederick, A.F.; Senior, M.M.; Lyons, B.A.; Black, S.; Kirschmeier, P.; Perkins, L.M.; & Wilson, O. (1996)
J Biomol NMR 7(2):89-98.
The Mechanism of Binding Staphylococcal Protein A to Immunoglobin G Does Not Involve Helix Unwinding.
Jendeberg, L.; Tashiro, M.; Tejero, R.; Lyons, B.A.; Uhlen, M.; Montelione, G.T.; & Nilsson, B. (1996)
Biochemistry 35(1):22-31.
An Improved Strategy for Determining Resonance Assignments for Isotopically Enriched Proteins and Its Application to an Engineered Domain of Staphylococcal Protein A.
Lyons, B.A.; Tashiro, M.; Cedergren, L.; Nilsson, B.; & Montelione, G.T. (1993)
Biochemistry 32(31):7839-45.
A General Approach for Determining Scalar Coupling Constants in Polypeptides and Proteins.
Montelione, G.T.; Emerson, S.D.; & Lyons, B.A. (1992)
Biopolymers 32(4):327-34.