References
1.) Zuckermann, R.N., “Peptoid Origins”, Pept. Sci., 2011, 96, 545-555
2.) Luxenhofer, R., Fetsch, C., Grossmann, A. “Polypeptoids: A Perfect Match for Molecular Definition and Macromolecular Engineering?” J Polym. Sci., 2013
3.) Zuckermann, R. N., Kodadek, T.,” Peptoids as Potential Therapeutics” Curr. Opin. Mol. Ther., 2009, 11, 299–307
4.) Sun, Jing, Zuckermann, R.N., “Peptoid Polymers: A Highly Designable Bioinspired Material”, ACS Nano Reviews, 2013, 7(6), 4715-4732
5.) Armand, P., Kirshenbaum, K., Falicov, A., Dunbrack, R. L., Dill, K. A., Zuckermann, R. N., Cohen, F. E., “Chiral N-Substituted Glycines Can Form Stable Helical Conformations.” Fold. Des. 1997, 369-375
6.) Zhang, D., Lahasky, S. H., Guo, L., Lee, C. U., Lavan, M., “Polypeptoid Materials: Current Status and Future Perspectives” Macromolecules, 2012, 45, 5833–5841
7.) Seo, J., Lee, B.C., Zuckermann, R.N., “Peptoids: Synthesis, Characterization and Nanostructures”, Comprehensive Biomaterials, 2011, 2, 53-76
8.) Alder, B.J., Wainwright, T.E., “Studies in Molecular Dynamics. I. General Method”, J.Chem.Phys., 1959, 31, 459-466
9.) Rapaport, D.C., “Molecular dynamics study of a polymer chain in solution”, J.Chem.Phys., 1979, 71, 3299-3303
10.) Smith, S. W., Hall, C.K., Freeman, B. D., “Molecular Dynamics for Polymeric Fluids Using Discontinuous Potentials”, J. Comp. Phys, 1997, 134, 16-30
11.) Zhou, Y., Zhang, C., Stell, G., Wang, J., “Temperature Dependence of the Distribution of the First Passage Time: Results from Discontinuous Molecular Dynamics Simulations of an All-Atom Model of the Second β-Hairpin Fragment of Protein G”, J. Am. Chem. Soc., 2003, 125(20), 6300-6305
12.) Strickland, L.A., Hall, C.K., Genzer, J., “Simulation of Mechanically-Assembled Monolayers In Poor Solvent Using Discontinuous Molecular Dynamics”, Macromolecules, 2010, 43(6), 3072-3080
13.) Cheon, M. Hall, C.K. “The Prime Model for Protein Aggregation: Extension to all 20 amino acids”, The 2008 Annual Meeting, AIChE
14.) Latshaw, D.C., Randolph, T.W., Hall, C.K., “Aggregation of amphipathic peptides at an aqueous–organic interface using coarse-grained simulations”, Mol. Sim., 2017, 43(17), 1448-1458
15.) Nguyen, H.D., Hall, C.K., “Phase diagrams describing fibrillization by polyalanine peptides”, Biophys. J., 2004, 87(6), 4122-4134
16.) Khan, M.A., Herbordt, M.C., “Parallel Discrete Molecular Dynamics Simulation with Speculation and In-Order Commitment”, J. Comp. Phys., 2011, 230(17), 6563-6582
17.) Shirvanyants, D., Ding, F., Tsao, D., Ramachandran, S. and Dokholyan, N.V., “Discrete Molecular Dynamics: An Efficient And Versatile Simulation Method For Fine Protein Characterization” J Phys. Chem. B, 2012, 116, 8375-8382.
18.) Mohle, K., Hofmann, H.J., “Peptides and peptoids—A systematic structure comparison”, J. Mol. Model., 1996, 2, 307–311
19.) Weiser, L.J., Santiso, E.E., “Molecular Modeling of Peptoid Polymers”, AIMS, Mat.Sci., 2017, 4(5), 1029-1051
20.) Crapster J.A., Guzei I.A., Blackwell H.E., “A Peptoid Ribbon Secondary Structure”, Angew. Chemie., 2013, 52, 5079–5084
21.) Mirijanian, D.T., Mannige, R.V., Zuckermann, R.N., Whitelam, S., “Development and use of an atomistic CHARMM‐based forcefield for peptoid simulation”, J. Comp. Chem., 2013, 35(5), 360-370
22.) Weiser, L.J., Santiso, E.E., “A CGenFF-Based Force Field for Simulations of Peptoids with both cis and trans Peptide Bonds”, J. Comp. Chem., submitted
23.) Prakash, A., Bare, M.D., Mundy, C.J., Pfaendtner, J., “Peptoid Backbone Flexibilility Dictates Its Interaction with Water and Surfaces: A Molecular Dynamics Investigation”, Biomacro., 2018, 19, 1006-1015
24.) Nguyen, H.D., Hall, C.K., “Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides”, PNAS, 2004, 101(46), 16180-16185
25.) Smith, A.V., Hall, C.K., “Bridging the gap between homopolymer and protein models: A discontinuous molecular dynamics study”, J. Chem. Phys., 2000, 113, 9331-9342
26.) Smith, A.V., Hall, C.K., “a-Helix Formation: Discontinuous Molecular Dynamics on an Intermediate-Resolution Protein Model”, Proteins: Structure, Function, Genetics, 2001, 44, 344-360