Colin's Publications in our lab
- Smith, CA, Shi, CA, Chroust, MK, Bliska, TE, Kelly, MJS, Jacobson, MP, Kortemme, T. Design of a Phosphorylatable PDZ Domain with Peptide-Specific Affinity Changes. Structure 21(1):54-64, 2013. doi: 10.1016/j.str.2012.10.007
- Ollikainen, N, Smith, CA, Fraser, JS, Kortemme, T. Chapter Four - Flexible Backbone Sampling Methods to Model and Design Protein Alternative Conformations in Methods in Enzymology Volume 523 (Methods in Protein Design):61-85, 2013. doi: 10.1016/B978-0-12-394292-0.00004-7
- Smith, CA, Kortemme, T. Predicting the Tolerated Sequences for Proteins and Protein Interfaces Using RosettaBackrub Flexible Backbone Design. PLoS ONE 6(7):e20451, 2011. doi:10.1371/journal.pone.0020451
- Leaver-Fay, A, Tyka, M, Lewis, SM, Lange, OF, Thompson, J, Jacak, R, Kaufman, KW, Renfrew, PD, Smith, CA, Sheffler, W, Davis, IW, Cooper, S, Treuille, A, Mandell, DJ, Richter, F, Ban, YA, Fleishman, SJ, Corn, JE, Kim, DE, Lyskov, S, Berrondo, M, Mentzer, S, Popović, Z, Havranek, JJ, Karanicolas, J, Das, R, Meiler, J, Kortemme, T, Gray, JJ, Kuhlman, B, Baker, D, Bradley, P. Chapter nineteen - Rosetta3: An Object-Oriented Software Suite for the Simulation and Design of Macromolecules in Methods in Enzymology Volume 487 (Computer Methods, Part C):545-74, 2011. doi: 10.1016/B978-0-12-381270-4.00019-6
- Smith, CA, Kortemme, T. Structure-Based Prediction of the Peptide Sequence Space Recognized by Natural and Synthetic PDZ Domains. J Mol Biol 402(2):460-74, 2010. doi:10.1016/j.jmb.2010.07.032
- Lauck, F, Smith, CA, Friedland, GD, Humphris, EL, Kortemme, T. RosettaBackrub—a web server for flexible backbone protein structure modeling and design. Nucleic Acids Res 38(suppl 2):W569-75, 2010. doi: 10.1093/nar/gkq369
- Friedland, GD, Linares, AJ, Smith, CA, Kortemme, T. A Simple Model of Backbone Flexibility Improves Modeling of Side-chain Conformational Variability. J Mol Biol 380(4):757-74, 2008. doi: 10.1016/j.jmb.2008.05.006
- Smith, CA, Kortemme, T. Backrub-Like Backbone Simulation Recapitulates Natural Protein Conformational Variability and Improves Mutant Side-Chain Prediction. J Mol Biol 380(4):742-56, 2008. doi: 10.1016/j.jmb.2008.05.023