Sri Rama Koti Ainavarapu

Tata Institute of Fundamental Research, Mumbai, Maharashtra, India 
"Sri Rama Koti Ainavarapu"
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Patra AP, Sharma S, Ainavarapu SR. (2016) Force spectroscopy of the Plasmodium falciparum vaccine candidate circumsporozoite protein suggests a mechanically pliable repeat region. The Journal of Biological Chemistry
Bera M, Ainavarapu SR, Sengupta K. (2016) Significance of 1B and 2B domains in modulating elastic properties of lamin A. Scientific Reports. 6: 27879
Bera M, Kotamarthi HC, Dutta S, et al. (2014) Characterization of unfolding mechanism of human lamin A Ig fold by single-molecule force spectroscopy-implications in EDMD. Biochemistry. 53: 7247-58
Ravi VK, Goel M, Kotamarthi HC, et al. (2014) Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregates. Plos One. 9: e87012
Kotamarthi HC, Sharma R, Narayan S, et al. (2013) Multiple unfolding pathways of leucine binding protein (LBP) probed by single-molecule force spectroscopy (SMFS). Journal of the American Chemical Society. 135: 14768-74
Aggarwal V, Kulothungan SR, Balamurali MM, et al. (2011) Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins. The Journal of Biological Chemistry. 286: 28056-65
Ainavarapu SR, Wiita AP, Huang HH, et al. (2008) A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding. Journal of the American Chemical Society. 130: 436-7
Szoszkiewicz R, Ainavarapu SR, Wiita AP, et al. (2008) Dwell time analysis of a single-molecule mechanochemical reaction. Langmuir : the Acs Journal of Surfaces and Colloids. 24: 1356-64
Ainavarapu SR, Brujic J, Huang HH, et al. (2007) Contour length and refolding rate of a small protein controlled by engineered disulfide bonds. Biophysical Journal. 92: 225-33
Perez-Jimenez R, Garcia-Manyes S, Ainavarapu SR, et al. (2006) Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy. The Journal of Biological Chemistry. 281: 40010-4
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