Michael Gromiha


Michael Gromiha


Computational studies on protein structure and functionComputer aided drug design


M Michael Gromiha received his Ph.D in Physics from Bharathidasan University, India and served as STA fellow, RIKEN Researcher, Research Scientist and Senior Scientist at Computational Biology Research Center, AIST, Japan till 2010. Currently, he is working as a Professor at Indian Institute of Technology (IIT) Madras, India. His main research interests are structural analysis, prediction, folding and stability of globular and membrane proteins, protein interactions and development of bioinformatics databases and tools. He has published over 200 research articles, 40 reviews, 5 editorials and a book on Protein Bioinformatics: From Sequence to Function by Elsevier/Academic Press. His papers received about 10,000 citations and h-index is 53. He is an Associate Editor of BMC Bioinformatics as well as Editorial Board Member of Scientific Reports, Biology Direct, Journal of Bioinformatics and Computational Biology and Current Computer Aided Drug design. He has received several awards including Oxford Uni-versity Press Bioinformatics prize, Okawa Science Foundation Research Grant, Young Scientist Travel awards from ISMB, JSPS, AMBO, ICTP etc., Best paper award at ICIC2011, ICTP Associateship award, ICMR International fellowship for Senior Biomedical Scientists, INSA senior scientist award, Best paper award in Bioinformatics by Department of Biotechnology, India, Institute Research and Development Award at IIT Madras, Outstanding Performance award from Initiative for Parallel Bioinformatics (IPAB), Tokyo Institute of Technology, Japan and Tamilnadu Scientist Award. He is a member of the National Academy of Sciences, India.


・Collaborative research with researchers at Tokyo Tech
・Indo-Japan joint projects
・Research discussions and advice students
・Deliver invited lectures
・Publish high quality papers in open access journals
・High performance computing
・Exchange visits


  • Development of computational tools for analysis and prediction of disease-causing mutations

  • Structural and molecular approach of targeting Bcl-2 family anti-apoptotic proteins

  • Predictive modeling of nucleic acid recognition dynamics and structured complex formation by disordered proteins

  • Deep learning in life sciences

  • Mutational effects on binding affinity of protein-protein complexes: development of a database, tools and applications to diseases

  • Prediction of disease-relevant mutations in transmembrane proteins


Research Scientist, AIST, Japan


Senior Research Scientist, AIST, Japan


Associate Professor, IIT Madras, India


ICTP Regular Associate, Italy


Specially Appointed Associate Professor, IIR,Tokyo Tech


Professor, IIT Madras, India


Specially Appointed Professor, IIR, Tokyo Tech


Specially Appointed Professor, School of Computing, Tokyo Tech


Oxford University Press Bioinformatics prize


Okawa Science Foundation Research Award


Indo-Australia Senior Scientist S&T Visiting Fellowship, INSA


ICMR International Fellowship for Senior Biomedical Scientists


Incentive award for best publications, Department of Biotechnology, India


Member, National Academy of Sciences, India

Outstanding performance award, Tokyo Institute of Technology


Institute Research and Development Award at mid-career level, IIT Madras


Michael Gromiha* and S. Selvaraj (2001). Comparison between Long-range Interactions and Contact Order in Determining the Folding Rate of Two-state Proteins: Application of Long Range Order to Folding Rate Prediction. J. Mol. Biol. 310, 27-32.


Michael Gromiha, J.G. Siebers, S. Selvaraj, H. Kono and A. Sarai (2004) Intermolecular and Intramolecular Readout Mechanisms in Protein-DNA Recognition. J. Mol. Biol. 337, 285-294.

Michael Gromiha* and S. Selvaraj (2004) Inter-residue Interactions in Protein Folding and Stability. Prog. Biophys. Mol. Biol. 86, 235-277.


Imai, M. Michael Gromiha and P. Horton (2008) Mitochondrial b-barrel proteins: an exclusive club. CELL 135, 1158-1159.


Michael Gromiha*, M.C. Pathak, K. Saraboji, E. Ortlund and E. Gaucher (2013) Hydrophobic environment is a key factor for the stability of thermophilic proteins. PROTEINS: Struct. Funct. Bioinf. 81:715-21.


M. Thangakani, S. Kumar, R. Nagarajan, D. Velmurugan and M. Michael Gromiha (2014) GAP: Towards almost hundred percent prediction for β-strand mediated aggregating peptides with distinct morphologies. Bioinformatics 30, 1983-1990.


Anoosha, L-T. Huang, R. Sakthivel, D. Karunagaran and M. Michael Gromiha* (2015) Discrimination of Driver and Passenger Mutations in Epidermal Growth Factor Receptor in Cancer. Mutation Res. 780: 24-34


Sandeep Kumar*, A. Mary Thangakani, R. Nagarajan, Satish K. Singh, D. Velmurugan andMichael Gromiha* (2016) Autoimmune Responses to Soluble Aggregates of Amyloidogenic Proteins Involved in Neurodegenerative Diseases: Overlapping Aggregation Prone and Autoimmunogenic regions. Scientific Reports 6: 22258


Michael Gromiha*, K. Yugandhar, and S. Jemimah (2017) Protein-protein interactions: scoring schemes and binding affinity. Current Opinion in Structural Biology, 44, 31-38.


Puneet Rawat, Sandeep Kumar, M.Michael Gromiha* (2018) An in-silico method for identifying aggregation rate enhancer and mitigator mutations in proteins. 
International Journal of Biological Macromolecules, 2018 Jun 24;118(Pt A):1157-1167.

Akila Parvathy Dharshini, Taguchi YH, Michael Gromiha M* (2018) Exploring the selective vulnerability in Alzheimer disease using tissue specific variant analysis. 
Genomics. 2018 Jun 4. pii: S0888-7543(18)30187-3

Shanmugam NRS, Selvin JFA, Veluraja K, Gromiha MM* (2018) Identification and Analysis of Key Residues Involved in Folding and Binding of Protein-carbohydrate Complexes. Protein Pept Lett., 2018;25(4):379-389

Kulandaisamy A, Binny Priya S, Sakthivel R, Tarnovskaya S, Bizin I, Hönigschmid P, Frishman D, Gromiha MM* (2018) MutHTP: mutations in human transmembrane proteins. Bioinformatics, 2018 Jul 1;34(13):2325-2326

Jemimah S, Gromiha MM* (2018) Exploring additivity effects of double mutations on the binding affinity of protein-protein complexes. Proteins. 2018 May;86(5):536-547