Sumudu P. Leelananda, Ph.D.
Affiliations: | 2011 | Biochemistry, Biophysics, and Molecular Biology | Iowa State University, Ames, IA, United States |
Area:
General Biophysics, Bioinformatics BiologyGoogle:
"Sumudu Leelananda"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Robert L. Jernigan | grad student | 2011 | Iowa State | |
| (Protein sequence-structure relationships.) | ||||
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Publications
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| Leelananda SP, Lindert S. (2019) Using NMR Chemical Shifts and Cryo-EM Density Restraints in Iterative Rosetta-MD Protein Structure Refinement. Journal of Chemical Information and Modeling |
| Leelananda SP, Lindert S. (2017) Iterative Molecular Dynamics-Rosetta Membrane Protein Structure Refinement Guided by Cryo-EM Densities. Journal of Chemical Theory and Computation |
| Kandoi G, Leelananda SP, Jernigan RL, et al. (2017) Predicting Protein Secondary Structure Using Consensus Data Mining (CDM) Based on Empirical Statistics and Evolutionary Information. Methods in Molecular Biology (Clifton, N.J.). 1484: 35-44 |
| Leelananda SP, Lindert S. (2016) Computational methods in drug discovery. Beilstein Journal of Organic Chemistry. 12: 2694-2718 |
| Leelananda SP, Kloczkowski A, Jernigan RL. (2016) Fold-specific sequence scoring improves protein sequence matching. Bmc Bioinformatics. 17: 328 |
| Leelananda SP, Jernigan RL, Kloczkowski A. (2016) Predicting Designability of Small Proteins from Graph Features of Contact Maps. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 23: 400-11 |
| Flatow D, Leelananda SP, Skliros A, et al. (2014) Volumes and surface areas: geometries and scaling relationships between coarse- grained and atomic structures. Current Pharmaceutical Design. 20: 1208-22 |
| Leelananda SP, Jernigan RL. (2013) Incorporating Protein Topology Information in Similarity Matrices for Improved Sequence Matching (A Fold-Specific Scoring System) Biophysical Journal. 104: 508a |
| Zimmermann MT, Leelananda SP, Kloczkowski A, et al. (2012) Combining statistical potentials with dynamics-based entropies improves selection from protein decoys and docking poses. The Journal of Physical Chemistry. B. 116: 6725-31 |
| Skliros A, Zimmermann MT, Chakraborty D, et al. (2012) The importance of slow motions for protein functional loops. Physical Biology. 9: 014001 |