PUBLICATIONS
In vitro glycosylation of the membrane protein γ-sarcoglycan in nanodiscs.
Harris, M.P., Dolan, R.S., Bryce, J.R., Ewusi, J.G., Cook, G.A.
ACS Omega (2023) 8: 40904-40910 [Abstract]
Relationship between cell envelope ultrastructure and the antibacterial properties of a novel hydrophobic eumelanin-inspired derivative.
Reed, D.R., Nehmzow, K., Essandoh, M.A., Ebqa’ai, M.A., Nelson, T.L., Lutter, E.I., Cook, G.A., Champlin, F.R.
Frontiers in Bacteriology (2023) 2: 1-11 [Abstract]
Recombinant expression, purification, and structural anaylsis of two ectodomains of Syndecan-1.
Anderson, A.R., Cook, G.A.
Protein Expression and Purificaiton (2023) 201: 106170 [Abstract]
EF-hand protein, EfhP, specifically binds Ca2+ and mediates Ca2+ regulation of virulence in a human pathogen Pseudomonas aeruginosa.
Kayastha, B.B., Kubo, A., Burch-Konda, J., Rogers, R.R., Dohmen, R.L., Bevere, J., Peng, S., Chaudhary, B., Mohanty, S. Barbier, M., Cook, G.A., Deng, J., Patrauchan, M.A.
Scientific Reports (2022) 12: 8791-8805 [Abstract]
In vitro glycosylation of membrane proteins using N-glycosyltransferase.
Liyanage, L., Harris, M.S., Cook, G.A.
ACS Omega (2021) 6: 12133-12142 [Abstract]
Expression, purification, and structural analysis of the full-length human integral membrane protein γ-sarcoglycan.
Jamaleddine, M., Harris, M.S., Liyanage, L., Cook, G.A.
Protein Expression and Purification (2020) 167: 105525 [Abstract]
The three-dimensional structure and drug interaction studies of HCV p7 in DHPC by solution NMR.
Cook, G.A., Dawson, L., Tian, Y., Opella, S.J.
Biochemistry (2013) 52: 5295-5303 [Abstract]
Structural and biophysical properties of a synthetic channel-forming peptide: designing a clinically relevant anion selective pore.
Cook, G.A., Shank, L.P., Seabra, M.B., Schultz, B.D., Iwamoto, T., Chen, J., Tomich,J.M.
Biochim. Biophys. Acta. (2012) 1818: 1039-48 [Abstract]
‘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.
Song, W.S., Park, S.H., Nothnagel, H.J., Lu, G.J., Wang, Y., Zhang, H., Cook, G.A., Howell, S.C., Opella, S.J.
J. Magn. Reson. (2012) 214:111-118 [Abstract]
Secondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis C virus by NMR spectroscopy.
Cook, G.A. and Opella, S.J.
Biochim. Biophys. Acta. (2011) 1808: 1448-53 [Abstract]
Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1.
Cook, G.A., Zhang, H., Park, S.H., Wang, Y., Opella, S.J.
Biochim. Biophys. Acta. (2011) 1808: 554-60 (peer reviewed, invited review) [Abstract]
Nanodiscs versus Macrodiscs for NMR of Membrane Protein.
Park, S.H., Berkamp, S., Cook, G.A., Chan, M.K., Viadiu, H., Opella, S.J.
Biochemistry (2011) 50:8983-5 [Abstract]
Expression and purification of the membrane protein p7 from HCV.
Cook, G.A., Stefer, S., Opella, S.J.
Peptide Science (2010) 96: 32-40 [Abstract]
NMR studies of membrane proteins, in Membrane Transporters in Drug Discovery and Development, Methods in Molecular Biology
Cook, G.A. and Opella, S.J.
Yan, Q., Ed, Springer, New York, (2010) pp. 263-275 (invited book chapter) [Abstract]
Structural characterization of two pore-forming peptides: Consequences of introducing a C-terminal tryptophan.
Herrera, A.I., Al-Rawi, A., Cook, G.A., Gao, J., Iwamoto, T., Prakash, O., Tomich, J.M., Chen, J.
Proteins (2010) 78:2238-50 [Abstract]
NMR studies of p7 protein from hepatitis C virus.
Cook, G.A. and Opella, S.J.
Eur. Biophys. J. (2009) 39:1097-104 (peer reviewed, invited review) [Abstract]
A strip-shield improves the efficiency of a solenoid coil in probes for high-field solid-state NMR of lossy biological samples.
Wu, C.H., Grant, C.V., Cook, G.A., Park S.H., Opella S.J.
J. Magn. Reson. (2009) 200:74-80 [Abstract]
NMR structure and dynamics studies of an anion binding channel-forming heptapeptide.
Cook, G.A., Pajewski, R., Aburi, M., Smith, P.E., Prakash, O., Tomich, J.M., Gokel, G.
J. Am. Chem. Soc. (2006) 128: 1633-1638 [Abstract]
Conformation and environment of channel-forming peptides: A Simulation Study.
Johnston, J.M., Cook, G.A., Samson, M.S., Tomich, J.M.
Biophys. J. (2006) 90: 1855-1864 [Abstract]
Redesigning channel-forming peptides: Amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity.
Shank, L.P., Broughman, J.R., , Takeguchi, W., Cook, G.A., Robbins, A.S., Hahn, L., Radke, G., Iwamoto, T., Schultz, B.D. and Tomich, J.M.
Biophys. J. (2006) 90:2138-2150 [Abstract]
Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor M2 segment.
Cook, G.A., Prakash, O., Zhang, K., Shank, L.P., Takeguchi, W.A., Robbins, A., Gong, Y.X., Iwamoto, T., Schultz, B.D., Tomich, J.M.
Biophy. J. (2004) 74:1424-1435 [Abstract]