Publications

Selected Publications

D.R. Weaver, K.G. Schaefer, and G.M. King,  Atomic force microscope kymograph analysis: A case study of two membrane proteins, Methods 223, 83-94 (2024). DOI: 10.1016/j.ymeth.2024.01.013 


G.A.K. Mensah, K.G. Schaefer, M.G. Bartlett, A.G. Roberts, and G.M. King, Drug-Induced Conformational Dynamics of P-Glycoprotein Underlies the Transport of Camptothecin Analogs, International Journal of Molecular Sciences 24, 16058 (2023). DOI:10.3390/ijms242216058  


K.G. Schaefer, A.G. Roberts & G.M. King, Advantages and potential limitations of applying AFM kymograph analysis to pharmaceutically relevant membrane proteins in lipid bilayers, Scientific Reports 13 (1), 11427 (2023). DOI: 10.1038/s41598-023-37910-7


D.R. Weaver & G.M. King, Atomic Force Microscopy Reveals Complexity Underlying General Secretory System Activity, International Journal of Molecular Sciences 24, 55 (2023). DOI: 10.3390/ijms24010055 


D.R. Weaver, D.N. Amin, & G.M. King, The conformations and basal conformational dynamics of translocation factor SecDF vary with translocon SecYEG interaction,  Journal of Biological Chemistry 298, 102412 (2022). DOI: 10.1016/j.jbc.2022.102412 

 

C.M. Russell*, K.G. Schaefer*, A. Dixson, A.L.H. Gray, R.J. Pyron, D.S. Alves, N. Moore, E.A. Conley, R.J. Schuck, T.A. White, T.D. Do, G.M. King, & F.N. Barrera, The Candida albicans virulence factor candidalysin polymerizes in solution to form membrane pores and damage epithelial cells,  eLife 11, e75490 (2022). *Equal contribution. DOI: 10.7554/eLife.75490


W.A. Alves, G.M. King & S. Guha, Looking into a crystal ball: printing and patterning self-assembled peptide nanostructures, Nanoscale 14, 15607 (2022).  DOI: 10.1039/D2NR03750E  


K.G. Schaefer, A.E. Pittman, F.N. Barrera, & G.M. King, Atomic force microscopy for quantitative understanding of peptide-induced lipid bilayer remodeling, Methods 197, 20 (2022). DOI: 10.1016/j.ymeth.2020.10.014

 

K.G. Schaefer, B. Grau, N. Moore, I. Mingarro, G.M. King, & F. Barrera, Controllable membrane remodeling by a modified fragment of the apoptotic protein Bax, Faraday Discussions 232, 114 (2021). DOI: 10.1039/D0FD00070A

 

G.M. King, & I. Kosztin, Towards a Quantitative Understanding of Protein Lipid Bilayer Interactions at the Single Molecule Level: Opportunities and Challenges, J. Membrane Biol 254, 17 (2021). DOI: 10.1007/s00232-020-00151-0

 

P.H. Nguyen, K.P. Sigdel, K.G. Schaefer, G.A.K. Mensah, G.M. King, & A.G. Roberts, The effects of anthracycline drugs on the conformational distribution of mouse P-glycoprotein explains their transport rate differences , Biochemical Pharmacology 174, 113813 (2020). DOI: 10.1016/j.bcp.2020.113813

        

T.R. Matin, M. Utjesanovic, K.P. Sigdel, V.F. Smith, I. Kosztin, & G.M. King, Characterizing the Locus of a Peripheral Membrane Protein-Lipid Bilayer Interaction Underlying Protein Export Activity in E. coli , Langmuir 36, 2143 (2020). DOI: 10.1021/acs.langmuir.9b03606

 

K. Chattrakun, D.P. Hoogerheide, C. Mao, L.L. Randall, & G.M. King, Protein Translocation Activity in Surface-Supported Lipid Bilayers , Langmuir 35, 12246 (2019). DOI: 10.1021/acs.langmuir.9b01928 [Also see Correction]

 

R.R. Sanganna Gari, K. Chattrakun, B.P. Marsh, C. Mao, N. Chada, L.L. Randall, & G.M. King Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers, Science Advances 5, eaav9404 (2019); DOI: 10.1126/sciadv.aav9404

 

S.Y. Kim, A.E. Pittman, E. Zapata-Mercado, G.M. King, W.C. Wimley, & K. Hristova, Mechanism of Action of Peptides That Cause the pH-Triggered Macromolecular Poration of Lipid Bilayers, Journal of the American Chemical Society 141, 6706 (2019); DOI: 10.1021/jacs.9b01970

 

M. Utjesanovic*, T.R. Matin*, K.P. Sigdel, G.M. King & I. Kosztin, Multiple stochastic pathways in forced peptide-lipid membrane detachment, Scientific Reports, 9, 451 (2019); *equal contribution; DOI: 10.1038/s41598-018-36528-4

 

N. Chada, K. Chattrakun, B.P. Marsh, C. Mao, P. Bariya, & G.M. King, Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis, Science Advances 4, eaat8797, (2018). DOI: 10.1126/sciadv.aat8797


K.P. Sigdel, L.A. Wilt, B.P. Marsh, A.G. Roberts, & G.M. King, The conformation and dynamics of P-glycoprotein in a lipid bilayer investigated by atomic force microscopy , Biochemical Pharmacology 156, 302 (2018). DOI: 10.1016/j.bcp.2018.08.017

 

A.E. Pittman, B.P. Marsh, & G.M. King, Conformations and dynamic transitions of a melittin derivative that forms macromolecule-sized pores in lipid bilayers , Langmuir 34, 8393 (2018). DOI: 10.1021/acs.langmuir.8b00804

 

K.P. Sigdel, A.E. Pittman, T.R. Matin, & G.M. King, High-Resolution AFM-Based Force Spectroscopy , Nanoscale Imaging, 49 (2018), In: Lyubchenko Y. (eds), Methods in Molecular Biology, vol 1814. Humana Press, New York, NY. DOI: 10.1007/978-1-4939-8591-3_4

 

S. Li, S.Y. Kim, A.E. Pittman, G.M. King, W.C. Wimley, & K. Hristova, Potent Macromolecule-Sized Poration of Lipid Bilayers by the Macrolittins, A Synthetically Evolved Family of Pore-Forming Peptides , Journal of the American Chemical Society 140, 6441 (2018); DOI: 10.1021/jacs.8b03026

 

B.P. Marsh, N. Chada, R.R. Sanganna Gari, K.P. Sigdel, & G.M. King, The Hessian Blob Algorithm: Precise Particle Detection in Atomic Force Microscopy Imagery; Scientific Reports 8, 978 (2018); DOI:10.1038/s41598-018-19379-x

 

T.R. Matin, K.P. Sigdel, M. Utjesanovic, B.P. Marsh, F. Gallazzi, V.F. Smith, I. Kosztin, & G.M. King, Single-molecule peptide-lipid affinity assay reveals interplay between solution structure and partitioning; Langmuir 33, 4057 (2017); DOI: 10.1021/acs.langmuir.7b00100

 

K.P. Sigdel and G.M. King, Force Detection for Microscopy Based on Direct Tip Trajectory Observation, United States Patent No.: 9,562,927, (2017).

 

N. Chada, K.P. Sigdel, R.R. Sanganna Gari, T.R. Matin, L.L. Randall, and G.M. King, Glass is a Viable Substrate for Precision Force Microscopy of Membrane Proteins; Scientific Reports 5; 12550 (2015); DOI: 10.1038/srep12550

 

Y. Zhao, et. al, Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and Development; Structure 23, 257 (2015); DOI: 10.1016/j.str.2014.11.021

 

A. Miskowiec, et. al, On the freezing behavior and diffusion of water in proximity to single-supported zwitterionic and anionic bilayer lipid membranes; Europhysics Letters 107, 28008 (2014); DOI:10.1209/0295-5075/107/28008

 

Y.G. Fulcher, R.R. Sanganna Gari, N.C. Frey, F. Zhang, R.J. Linhardt, G.M. King, and S.R. Van Doren, Heparinoids Activate a Protease, Secreted by Mucosa and Tumors, via Tethering Supplemented by Allostery; ACS Chemical Biology 9, 957 (2014); DOI: 10.1021/cb400898t

 

K.P. Sigdel, J.S. Grayer, and G.M. King, Three Dimensional Atomic Force Microscopy: Interaction Force Vector by Direct Observation of Tip Trajectory; Nano Letters 13, 5106 (2013); DOI: 10.1021/nl403423p

 

C. Mao, C. Cheadle, S.J.S. Hardy, A.A. Lily, Y. Suo, R.R. Sanganna Gari, G.M. King, and L.L. Randall, Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species; Proceedings of the National Academy of Sciences of the United States of America 110, 11815 (2013); DOI: 10.1073/pnas.1303289110

 

R.R. Sanganna Gari, N.C. Frey, C. Mao, L.L. Randall, and G.M. King, Dynamic Structure of the Translocon SecYEG in Membrane: Direct Single Molecule Observations; Journal of Biological Chemistry 288, 16848 (2013); DOI: 10.1074/jbc.M113.471870

 

A.B. Churnside, R.M. Sullan, D.M. Nguyen, S.O. Case, M. S. Bull, G.M. King, and T.T. Perkins, Routine and timely sub-picoNewton force stability and precision for biological applications of atomic force microscopy; Nano Letters 12, 3557 (2012); DOI: 10.1021/nl301166w

 

N.B. Ukah, J. Granstrom, R.R. Sanganna Gari, G.M. King, S. Guha, Low-operating voltage and stable organic field-effect transistors with poly (methyl methacrylate) gate dielectric solution deposited from a high dipole moment solvent; Applied Physics Letters 99, 243302 (2011); DOI: 10.1063/1.3669696

 

A.B. Churnside, G.M. King, and T.T. Perkins, Label-free optical imaging of membrane patches for atomic force microscopy; Optics Express 18, 23924 (2010); DOI: 10.1063/1.3669696

 

G.M. King, A.R. Carter, A.B. Churnside, L.S. Eberle, and T.T. Perkins, Ultrastable atomic force microscopy: atomic-scale stability and registration in ambient conditions; Nano Letters 9, 1451 (2009); DOI: 10.1021/nl803298q


A.R. Carter, G.M. King, and T.T. Perkins, Back-scattered detection provides atomic-scale localization precision, stability, and registration in 3D; Optics Express 15, 13434 (2007); DOI: 10.1364/OE.15.013434


A.R Carter, G.M. King, T.A. Sheard, W. Halsey, D. Alchenberger & T.T. Perkins, Stabilization of an optical microscope to 0.1 nm in 3D; Applied Optics 46,421 (2007); DOI: 10.1364/AO.46.000421


G.M. King and J.A. Golovchenko Probing nanotube-nanopore interactions; Physical Review Letters 95, 216103 (2005)


G.M. King, G. Schurmann, D. Branton and J.A. Golovchenko, Nanometer patterning with ice; Nano Letters 5, 1157 (2005)


H.B. Peng, T.G. Ristroph,  G.M. Schurmann, G.M. King, J. Yoon, V. Narayanamurti, and J. A. Golovchenko, Patterned Growth of Single Walled Carbon Nanotube Arrays from a vapor-deposited Fe Catalyst; Applied Physics Letters 83, 4238 (2003)


G. M. King, J. S. Lamb, and G. Nunes, Jr., Quartz tuning forks as sensors for attractive-mode force microscopy under ambient conditions; Applied Physics Letters 79, 1712 (2001)


G. M. King and G. Nunes, Jr., Attractive-mode force microscope for investigations of biomolecules under ambient conditions; Review of Scientific Instruments 72, 4261 (2001)