Three popular force fields predict consensus mechanism of Aβ peptide binding to the DMPC bilayer.

Lockhart, C., Smith, A. K., & Klimov, D. K. (2020) Three popular force fields predict consensus mechanism of Aβ peptide binding to the DMPC bilayer. J. Chem. Inf. Model. 60(40): 2282-2293, doi: 10.1021/acs.jcim.0c00096

Do cholesterol and sphingomyelin change the mechanism of Aβ25-35 peptide binding to zwitterionic bilayer?

Smith, A. K., Khayat, E., Lockhart, C., & Klimov, D. K. (2019) Do cholesterol and sphingomyelin change the mechanism of Aβ25-35 peptide binding to zwitterionic bilayer? J. Chem. Inf. Model. 59(12): 5207-5217, doi: 10.1021/acs.jcim.9b00763

Cholesterol changes the mechanism of Aβ peptide binding to the DMPC bilayer.

Lockhart, C. & Klimov, D. K. (2017) Cholesterol changes the mechanism of Aβ peptide binding to the DMPC bilayer. J. Chem. Inf. Model. 57(10): 2554-2565, doi: 10.1021/acs.jcim.7b00431

Is the conformational ensemble of Alzheimer's Aβ10-40 peptide force field dependent?

Ciwy, C. M., Lockhart, C., & Klimov, D. K. (2017) Is the conformational ensemble of Alzheimer's Aβ10-40 peptide force field dependent? PLoS Comput. Biol. 13(1): e1005314, doi: 10.1371/journal.pcbi.1005314

Does replica exchange with solute tempering efficiently sample Aβ peptide conformational ensembles?

Smith, A. K., Lockhart, C., & Klimov, D. K. (2016) Does replica exchange with solute tempering efficiently sample Aβ peptide conformational ensembles? J. Chem. Theory Comput. 12(10): 5201-5214, doi: 10.1021/acs.jctc.6b00660

The Alzheimer's disease Aβ peptide binds to the anionic DMPS lipid bilayer.

Lockhart, C. & Klimov, D. K. (2016) The Alzheimer's disease Aβ peptide binds to the anionic DMPS lipid bilayer. Biochim. Biophys. Acta 1858(6): 1118-1128, doi: 10.1016/j.bbamem.2016.03.001

Greedy replica exchange algorithm for heterogeneous computing grids.

Lockhart, C., O'Connor, J., Armentrout, S., & Klimov, D. K. (2015) Greedy replica exchange algorithm for heterogeneous computing grids. J. Mol. Model. 21(9): 243, doi: 10.1007/s00894-015-2763-5

Calcium enhances binding of Aβ monomer to DMPC bilayer.

Lockhart, C. & Klimov, D. K. (2015) Calcium enhances binding of Aβ monomer to DMPC bilayer. Biophys. J. 108(7): 1807-1818, doi: 10.1016/j.bpj.2015.03.001

Binding of Aβ peptide creates lipid density depression in DMPC bilayer.

Lockhart, C. & Klimov, D. K. (2014) Binding of Aβ peptide creates lipid density depression in DMPC bilayer. Biochim. Biophys. Acta 1838(10): 2678-2688, doi: 10.1016/j.bbamem.2014.07.010

Alzheimer's Aβ10-40 peptide binds and penetrates DMPC bilayer: an isobaric-isothermal replica exchange molecular dynamics study.

Lockhart, C. & Klimov, D. K. (2014) Alzheimer's Aβ10-40 peptide binds and penetrates DMPC bilayer: An isobaric-isothermal replica exchange molecular dynamics study. J. Phys. Chem. B 118(10): 2638-2648, doi: 10.1021/jp412153s

Revealing hidden helix propensity in Aβ peptide by molecular dynamics simulations.

Lockhart, C. & Klimov, D. K. (2013) Revealing hidden helix propensity in Aβ peptide by molecular dynamics simulations. J. Phys. Chem. B 117(40): 12030-12038, doi: 10.1021/jp407705j

Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.

Lockhart, C. & Klimov, D. K. (2012) Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide. Biophys. J. 103(11): 2341-2351, doi: 10.1016/j.bpj.2012.10.003

Explicit solvent molecular dynamics simulations of Aβ peptide interacting with ibuprofen ligands.

Lockhart, C., Kim, S., & Klimov, D. K. (2012) Explicit solvent molecular dynamics simulations of Aβ peptide interacting with ibuprofen ligands. J. Phys. Chem. B 116(43): 12922-12932, doi: 10.1021/jp306208n

Does amino acid sequence determine the properties of Aβ dimer?

Lockhart, C., Kim, S., Kumar, R., & Klimov, D. K. (2011) Does amino acid sequence determine the properties of Aβ dimer? J. Chem. Phys. 135: 035103, doi: 10.1063/1.3610427