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imageOur EffortsWe are studying the effects of post-translational modification on membrane proteins involved human diseases. We use in vitro glycosylation to study the changes that occur when a sugar group is attached to a protein. Read More
imageOur Methods We use both solution and solid-state NMR to determine the structure, dynamics and interactions of membrane proteins in lipid enviroments that resemble the membranes of cells. Read More
imageRecent Presentations Leshani Adelaide Liyanage recently presented work she had done with undergraduate Michael Jamaleddine at the Pentasectional ACS Meeting in Tulsa, Oklahoma. The title of her talk was "in vitro Glycosylation of the Membrane Glycoprotein γ-Sarcoglycan". Read More
imageNews Three senior students from the Cook Lab were hooded in the Honors College Hooding Ceremony. Eston Blair, Libby Caldwell and Michael Jamaleddine were recognized. Read More

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Take a virtual tour of our lab in the Henry Bellmon Research Center

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The goal of our lab is to use multidisciplines of science; chemistry, biology, biochemistry, and physics, to improve the quality of life for mankind. We believe that we can make a difference with our research.










Selected Publications

Three-dimensional structure and interaction studies of hepatitis C virus p7 in 1,2-dihexanoyl-sn-glycero-3-phosphocholine by solution nuclear magnetic resonance Biochemistry, 2013, 52:5295-303 Cook GA, Dawson LA, Tian, Y, Opella, SJ


'q-Titration' of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy J Magn Reson, 2012 214:111-8 Son WS, Park SH, Nothnagel HJ, Lu GJ, Wang Y, Zhang H, Cook GA, Howell SC, Opella SJ


Nanodiscs versus macrodiscs for NMR of membrane proteins Biochemistry, 2011, 50:8983-5 Park SH, Berkamp S, Cook GA, Chan MK, Viadiu H, Opella SJ


Structural and biophysical properties of a synthetic channel-forming peptide: designing a clinically relevant anion selective pore Biochim Biophys Acta, 2012, 1818:1039-48 Bukovnik U1, Gao J, Cook GA, Shank LP, Seabra MB, Schultz BD, Iwamoto T, Chen J, Tomich JM