Publications‎ > ‎


  • Staller, M.V., Holehouse, A.S., Swain-Lenz, D., Das, R.K., Pappu, R.V., Cohen, B.A. (2018). A deep mutational scan of an acidic activation domain. Cell Systems, (In press)
  • Sherry, K., Das, R. K., Pappu, R.V., & Barrick, D. (2017). Control of Transcriptional Activity by Design of Charge Patterning in the Intrinsically Disordered RAM Region of the Notch Receptor. Proceedings of the National Academy of Sciences, USA, (Selected and Evaluated by Faculty of 1000PDF
  • Holehouse, A.S., Das, R. K., Ahad, J. N., Richardson, M. O. G. , & Pappu, R. V.  (2017). CIDER: Resources to Analyze and Classify Sequence-Ensemble Relationships of Intrinsically Disordered Proteins. Biophysical Journal, 112, 16-21. PDF
  • Das, R.K. , Huang, Y. , Phillips, A.H. , Kriwacki, R.W. , & Pappu, R.V. (2016). Cryptic Sequence Features within the Disordered Protein p27Kip1 Regulate Cell Cycle Signaling. Proceedings of the National Academy of Sciences, USA, 113(20), 5616-5621. PDF
  • Gruet. A., Dosnon, M., Blocquel, D., Brunel J., Gerlier, D., Das, R.K., Bonetti, D., Gianni, S., Fuxreiter, M., Longhi, S., & Bignon, C. (2016). Fuzzy Regions in an Intrinsically Disordered Protein Impair Protein-Protein Interactions. The FEBS Journal, 283, 576-594. (Editor's Choice paper; Selected and Evaluated by Faculty of 1000PDF 
  • Das, R. K., Ruff, K., & Pappu, R.V. (2015). Relating Sequence Encoded Information to Form and Function of Intrinsically Disordered Proteins. Current Opinion in Structural Biology, 32, 102–112. PDF
  • Das, R.K. & Pappu, R.V. (2013). Conformations of Intrinsically Disordered Proteins are influenced by the Linear Sequence Distribution of Oppositely Charged Residues. Proceedings of the National Academy of Sciences, USA110(33), 13392-13397. PDF
  • Lyle, N.J., Das, R.K., & Pappu, R.V. (2013). A Quantitative Measure of Protein Conformational Heterogeneity. Journal of Chemical Physics, 139(121907), 1-12. PDF
  • Das, R.K., Mittal, A., & Pappu, R.V. (2013). Achieving Specific Recognition through Disordered Regions. BioEssays, 35(1), 17-22. PDF
  • Das, R.K., Mao, A.H., & Pappu, R.V. (2012). Unmasking Functional Motifs within Disordered Regions of Proteins. Science Signaling, 5(220), pe17, 1-3. PDF
  • Das, R.K., Crick, S.L., & Pappu, R.V. (2012). N-terminal Segments Modulate the α-Helical Propensities of Intrinsically Disordered Basic Regions of bZIP Proteins.  Journal of Molecular Biology, 416(2), 287-299. (Selected and Evaluated by Faculty of 1000PDF
  • Driver, J.W., Rogers, A.R., Jamison, D.K., Das, R.K., Kolomeisky, A.B., & Diehl MR (2010). Coupling between Motor Proteins Determines Dynamic Behaviors of Motor Protein Assemblies. Physical Chemistry Chemical Physics, 12(35), 10398-10405. PDF
  • Das, R.K. & Kolomeisky, A.B. (2010). Facilitated Search of Proteins on DNA: Correlations are Important. Physical Chemistry Chemical Physics, 12(12), 2999- 3004. PDF
  • Das, R.K. & Kolomeisky, A.B. (2009). Dynamic Properties of Molecular Motors in the Divided-Pathway Model. Physical Chemistry Chemical Physics, 11(24), 4815-4820. PDF
  • Das, R.K. & Kolomeisky, A.B. (2008). Spatial Fluctuations Affect the Dynamics of Motor Proteins. Journal of Physical Chemistry B, 112(35), 11112-11121. PDF
  • Das, R.K. & Kolomeisky, A.B. (2008). Interaction between Motor Domains Can Explain Complex Dynamics of Heterodimeric Kinesins. Physical Review E, 77(6), 061912-16. PDF
  • Banerjee, A., Mukherjee, S., Verma, R.K.,  Jana, B.,  Khand, T.K., Chakroborty, M., Das, R.K., Biswas, S., Saxena, A., Singh, V., Hallen, R.M., Rajput, R.S., Tewari, P., Kumar, S., Saxena, V.,  Ghosh, A.K.,  John, J., & Gupta-Bhaya P. (2007). Fiber Optic Sensing of Liquid Refractive Index, Sensors and Actuators B 123(1), 594-605. PDF

Book Chapter:
  • Mittal A., Das, R.K. (co-first author), Vitalis, A., & Pappu, R.V. (2015). ABSINTH Implicit Solvation Model and Force Field Paradigm for Use in Simulations of Intrinsically Disordered Proteins. Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods, ed Fuxreiter M (CRC Press), pp 181–203. 1st Ed.