Wellcome Trust-DBT Intermediate Fellow,

Ramanujan Fellow


Ph. D

National Centre for Biological Sciences-TIFR (NCBS-TIFR), Bangalore 

Postdoctoral Fellow

Harvard University, USA 






Eukaryotic genomes are packaged as chromatin within the cell nucleus. Chromatin has a multiscale three-dimensional architecture varying from nucleosomes, loops, topologically associating domains to chromosome territories. The three-dimensional organization of chromatin within the nuclear space has been linked with genome function like regulation of gene expression and other DNA associated processes. Although application of various methods continue to provide fine details of chromatin architecture but the principles governing the three-dimensional organization of chromatin are just beginning to unravel. We are interested in understanding the role of chromatin-associated proteins in regulating chromatin organization at different genomic and special scales, from nucleosome positioning/accessibility to chromatin topology. To address this problem we are using an interdisciplinary approach including protein biochemistry/biophysics, genome wide sequencing based methods (like ChIP-seq, Chromosome conformation capture, MNase-seq and RNA-seq), mass spectrometry to polymer modeling.  


                                                  Multiscale organization of genome

Group Members:

Yonous Bhat (Ph. D student)

Fouziya Shah (Ph. D student) 

Adfar Amin    (Ph. D student)





1. Shah, F. R.,  Bhat, Y. A. & Wani, A. H.* Subnuclear distribution of proteins: Links with genome architecture. Nucleus (2017, In Press)


2.Wani, A. H., Boettiger, A. N., Shorderet, P., Ergun, A., Munger, C., Saderyev, R. I., Zhuang, X., Kingston, R. E. & Francis, N. J. * Chromatin topology is coupled to Polycomb Group protein subnuclear organization. Nature Commu., 2016 7:10291doi: 10.1038/ncomms10291.


3. Follmer. N. E., Wani, A. H., & Francis, N. J. *. Polycomb group proteins remain bound at specific sites during mitosis. PloS Genetics. 2012, 8,12: e1003135.


4. Wani, A. H. and Udgaonkar, J. B.* Mass spectrometry studies of protein folding. Current Science, 2012, 102, 2, 245-265. 


5. Wani, A. H. and Udgaonkar, J. B. *  Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration. Proc Natl Acad Sci USA. 2009, 106, 49: 20711-20716.


6. Wani, A. H. and Udgaonkar, J. B. *  Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase. Journal of Molecular Biology, 2009, 387, 2: 348-362.


7. Wani, A. H. and Udgaonkar, J. B. *  HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH. Biochemistry, 2006,45, 37, 11226-11238


8. Modi, S., Wani, A. H.  & Krishnan Y. * The PNA-DNA hybrid I-motif: implications for sugar-sugar contacts in i-motif tetramerization. Nucleic acids research, 2006, 34, 16, 4354-4363.





  1. Awarded Wellcome Trust-DBT intermediate fellowship by Wellcome Trust-DBT India Alliance.  (2016)  
  1. Awarded Early Career Research Award by Department of Science and Technology, India.  (2016)    
  1. Awarded Ramanujan fellowship by Department of Science and Technology, India.   (2014)