Michael J. Schnieders, DSc

Assistant Professor of Biochemistry
Assistant Professor of Biomedical Engineering
Assistant Professor of Biochemistry
Assistant Professor of Biomedical Engineering (BME)

Contact Information

Office: 5013 Seamans Center for the Engineering Arts and Sciences
Iowa City, IA 52242

Primary Office: 4-516 Bowen Science Building
Iowa City, IA 52242

Lab: 4-508 Bowen Science Building
Iowa City, IA 52242



DSc, Biomedical Engineering, Washington University in St. Louis

Post Doctoral Fellow, Chemistry, Stanford University
Post Doctoral Fellow, Biomedical Engineering, The University of Texas

Education/Training Program Affiliations

Department of Biochemistry PhD, Department of Pharmacology Graduate Program, Interdisciplinary Graduate Program in Informatics, Medical Scientist Training Program

Center, Program and Institute Affiliations

Center for Biocatalysis and Bioprocessing, Center for Bioinformatics and Computational Biology, Holden Comprehensive Cancer Center, Institute for Vision Research, Iowa Institute of Human Genetics.

Research Summary

Our lab is focused on molecular biophysics theory and high performance computational algorithms that are needed to reduce the time and cost of engineering drugs and organic biomaterials. A complementary goal is to help open the door to personalized medicine by developing tools to map genetic information onto molecular phenotypes.

1. Next Generation Macromolecular X-ray Crystallography X-ray crystallography is a critical experimental method used by biochemists to determine the structure and function of the biomolecular foundations of medicine. We have recently demonstrated that the chemical information contained in a polarizable force field called AMOBEA significantly improves DNA and protein structures compared to X-ray refinements done with previous generation theory. We are now working to model experimental X-ray diffraction data as an ensemble using Bayesian inference.

2. Prediction of the Structure, Thermodynamics and Solubility of Drug Tablets Important unsolved problems for the engineering of organic biomaterials include prediction of their structure, thermodynamic stability and solubility from first principles. Solubility is the saturating concentration of a molecule within a liquid solvent, where the physical process consists of solvated molecules in equilibrium with their solid phase. We have developed the first consistent procedure for the prediction of the structure, thermodynamic stability, and solubility of organic crystals using molecular dynamics simulations. Currently the methodology is being extended to predict the properties for a range of organic crystals, including both pharmaceuticals and peptide models of neurological aggregation diseases.

3. Personalized Medicine: From Genome Sequencing to Molecular Phenotypes Since 2001, the cost to sequence a patient’s genome has fallen from $100 million to approximately $1,000. The rapid achievement of affordable genetic information is outpacing our ability to fully capitalize on opportunities to provide personalized healthcare. To help address this challenge, we are collaborating with The University of Iowa Center for Bioinformatics and Computational Biology to develop tools that tightly couple bioinformatics to the computational prediction of biomolecular structure, thermodynamics and kinetics.

4. Biomolecular Electrostatics and High-Performance Computing Application such as X-ray crystallography refinement, biomaterials thermodynamics and personalized medicine depend on an accurate, efficient description of molecular energetics. Our lab contributes a parallelized molecular biophysics computer code called Force Field X that includes novel biomolecular electrostatics algorithms such as particle-mesh Ewald with support for space group symmetry and the generalized Kirkwood implicit solvent model.


Simpson, A., Avdic, A., Roos, B. R., DeLuca, A., Miller, K., Schnieders, M. J., Scheetz, T. E., Alward, W. L. & Fingert, J. H. (2017). LADD syndrome with glaucoma is caused by a novel gene. Molecular Vision, 23, 179-184.

Lansdon, L. A., Bernabe, H. V., Nidey, N., Standley, J., Schnieders, M. J. & Murray, J. C. (2017). The Use of Variant Maps to Explore Domain-Specific Mutations of FGFR1. Journal of Dental Research, 96(11), 1339-1345. DOI: 10.1177/0022034517726496.

Ren, P., Chun, J., Thomas, D. G., Schnieders, M. J., Marucho, M., Zhang, J. & Baker, N. A. (2012). Biomolecular electrostatics and solvation: a computational perspective. Quarterly Reviews of Biophysics, 45(4), 427-491. PMID: 23217364.

Schnieders, M. J., Kaoud, T. S., Yan, C., Dalby, K. N. & Ren, P. (2012). Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinases. Current Pharmaceutical Design, 18(9), 1173-1185. PMID: 22316156.

Schnieders, M. J., Fenn, T. D. & Pande, V. S. (2011). Polarizable atomic multipole X-ray refinement: Particle mesh Ewald electrostatics for macromolecular crystals. Journal of Chemical Theory and Computation, 7(4), 1141-1156. DOI: 10.1021/ct100506d.

MacCallum, J. L., Pérez, A., Schnieders, M. J., Hua, L., Jacobson, M. P. & Dill, K. A. (2011). Assessment of protein structure refinement in CASP9. Proteins: Structure, Function, and Bioinformatics, 79(S10), 74-90. PMID: 22069034.

Fenn, T. D., Schnieders, M. J., Mustyakimov, M., Wu, C., Langan, P., Pande, V. S. & Brunger, A. T. (2011). Reintroducing electrostatics into macromolecular crystallographic refinement: application to neutron crystallography and DNA hydration. Structure, 19(4), 523-533. PMID: 21481775.

Fenn, T. D., Schnieders, M. J. (2011). Polarizable atomic multipole X-ray refinement: weighting schemes for macromolecular diffraction. Acta Crystallographica Section D, 67(11), 957-965. PMID: 22101822.

Fenn, T. D., Schnieders, M. J., Brunger, A. T. & Pande, V. S. (2010). Polarizable atomic multipole x-ray refinement: hydration geometry and application to macromolecules. Biophysical Journal, 98(12), 2984-2992. PMID: 20550911.

Mathew-Fenn, R. S., Das, R., Fenn, T. D., Schnieders, M. J. & Harbury, P. (2009). Response to comment on "Remeasuring the double helix". Science, 325(5940), 538. DOI: 10.1126/science.1168876.

MacCallum, J. L., Hua, L., Schnieders, M. J., Pande, V. S., Jacobson, M. P. & Dill, K. A. (2009). Assessment of the protein-structure refinement category in CASP8. Proteins: Structure, Function, and Bioinformatics, 77(S9), 66-80. PMID: 19714776.

Shi, Y., Jiao, D., Schnieders, M. J. & Ren, P. (2009). Trypsin-ligand binding free energy calculation with AMOEBA. Conference proceedings: Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Conference, 2009, 2328-31. PMID: 19965178.

Anderson, D. A., Schnieders, M. J., Heiner, A. D., Pederson, D. R., Brown, T. D. & Brand, R. A. (1999). A surgical guide to accurately place pins or nails within the femoral head. Journal of Musculoskeletal Research, 3, 233-237. DOI: 10.1142/S0218957799000245.