Humboldt Award for Ken Brown

School of Chemistry and Biochemistry Professor Ken Brown will partner with colleagues in Germany to help develop molecular quantum logic spectroscopy.

Colorful and Dynamic Workshops

School of Chemistry and Biochemistry Professor Rigoberto Hernandez and Research Scientist Kyril Solntsev are organizing unique workshops in the mountains.

School of Chemistry and Biochemistry to Host Charles L. Liotta Symposium

This year marks Regents Professor Emeritus Charles Liotta’s 50th at Georgia Tech, and the celebration is on.

Seminars & Events

Prof. Julie S. Biteen - University of Michigan
Colloquium - Thursday, January 29, 2015 - 4:00pm - MoSE G011
Frontiers in Science - Lee Dugatkin - University of Louisville
Special Seminar - Thursday, January 29, 2015 - 7:00pm - Clary Theatre, Bill Moore Student Success Center
Prof. Leslie Murray - University of Florida
Inorganic Division Seminar - Tuesday, February 3, 2015 - 4:00pm - MoSE 3201A
Meeting - Thursday, February 5, 2015 - 11:00am - MoSE 3201A

Featured Research

Article Title
Research Authors
Kaczanowska, K.., Harel, M.., Radic, Z.., Changeux, J.., Finn, M.., Taylor, P..
Proceedings of the National Academy of Sciences, U.S.A. (2014), Vol. 111, 10749-10754
Miscellaneous Details
The work was supported by National Institutes of Health Grant GM 18360-40 (to P.T.), the Tobacco-related Disease Research Program 21FT_0024 (to K.K.), and the Kavli Institute for Brain and Mind to (J.-P.C.).

The nicotinic acetylcholine receptor (nAChR) and the acetylcholine binding protein (AChBP) are pentameric oligomers in which binding sites for nicotinic agonists and competitive antagonists are found at selected subunit interfaces. The nAChR spontaneously exists in multiple conformations associated with its activation and desensitization steps, and conformations are selectively stabilized by binding of agonists and antagonists. In the nAChR, agonist binding and the associated conformational changes accompanying activation and desensitization are cooperative. AChBP, which lacks the transmembrane spanning and cytoplasmic domains, serves as a homology model of the extracellular domain of the nAChRs. We identified unique cooperative binding behavior of a number of 4,6-disubstituted 2-aminopyrimidines to Lymnaea AChBP, with different molecular variants exhibiting positive, nH > 1.0, and negative cooperativity, nH < 1.0. Therefore, for a distinctive set of ligands, the extracellular domain of a nAChR surrogate suffices to accommodate cooperative interactions. X-ray crystal structures of AChBP complexes with examples of each allowed the identification of structural features in the ligands that confer differences in cooperative behavior. Both sets of molecules bind at the agonist- antagonist site, as expected from their competition with epibatidine. An analysis of AChBP quaternary structure shows that cooperative ligand binding is associated with a blooming or flare conformation, a structural change not observed with the classical, noncooperative, nicotinic ligands. Positively and negatively cooperative ligands exhibited unique features in the detailed binding determinants and poses of the complexes.

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