Gordon S. Rule -Department of Biological Sciences - Carnegie Mellon University

Gordon S. Rule


246 Mellon Institute
Department of Biological Sciences
Carnegie Mellon University
4400 Fifth Avenue
Pittsburgh, PA 15213
Phone: 412-268-1839
Fax: 412-268-7129


Ph.D., Carnegie Mellon University
Postdoctoral Appointment, Stanford University


My research is directed at understanding inter-molecular interactions in biological systems. An understanding of these interactions is required if biological systems are to be comprehended at the molecular level. The combined tools of molecular biology, computational biology, NMR spectroscopy and x-ray crystallography are used to provide important information to aid in our understanding of these interactions. Our research efforts have been directed at enzyme-substrate interactions, protein-lipid interactions, antibody-antigen interactions, RNA structure, and protein-nucleic acid interactions. Current areas of research are briefly described below.

Enzyme-Substrate Interactions: Glutathione transferases are cellular detoxification enzymes. As such, they play an important role in the protection of an organism from carcinogens and other toxic chemicals. Current efforts in my laboratory are directed at correlating substrate specificity and enzymatic mechanism with protein dynamics and substrate-protein interactions.

Dynamics of scFv-Fluorescent dye complexes: As part of a team designing new biosensors we are using NMR techniques to investigate the role of protein dynamics in the generation of fluorescence from dyes bound to single chain antibody fragments.

Automated NMR assignments: A key bottleneck in the analysis of NMR data is the assignment of resonance lines to atoms in the protein. We are developing automated Monte-carlo methods to accomplish this task.


Sinha K, Jen-Jacobson L, Rule GS. Divide and conquer is always best: sensitivity of methyl correlation experiments. J Biomol NMR. 2013 Jun 15.

Senutovitch N, Stanfield RL, Bhattacharyya S, Rule GS, Wilson IA, Armitage BA, Waggoner AS, Berget PB. A variable light domain fluorogen activating protein homodimerizes to activate dimethylindole red. Biochemistry. 2012 Mar 27;51(12):2471-85. Epub 2012 Mar 14.

Sinha K, Jen-Jacobson L, Rule GS. Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes. Biochemistry. 2011 Nov 29;50(47):10189-91. Epub 2011 Nov 3.

Hitchens TK, Zhan Y, Richardson LV, Richardson JP and Rule GS. Sequence-specific interactions in the RNA-binding domain of Escherichia coli transcription termination factor Rho.J Biol Chem., 281:33697-703, 2006.

Zhan Y and Rule GS. Stable triplet of uracil-uracil basepairs in a small antisense RNA.J Am Chem Soc., 127:15714-5, 2005.

Zhan Y and Rule GS. Glutathione induces helical formation in the carboxy terminus of human glutathione transferase A1-1.Biochemistry, 43:7244-54, 2004.

Hitchens TK, Lukin JA, Zhan Y, McCallum SA and Rule GS. MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins. J Biomol NMR, 25:1-9, 2003.

McCallum SA, Hitchens TK, Torborg C and Rule GS. Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase. Biochemistry, 39:7343-56, 2000.

Full PubMed Listings