Hema Chandra Kotamarthi

Affiliations: 
IIT Madras 
Area:
Biophysical chemistry
Website:
https://hckotamarthi.wixsite.com/hckbiophysicallab
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"Hema Kotamarthi"
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Publications

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Kasal MR, Kotamarthi HC, Johnson MM, et al. (2023) Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease. Cell Reports. 42: 113061
Mukherjee S, Mepperi J, Sahu P, et al. (2022) Single-Molecule Optical Tweezers As a Tool for Delineating the Mechanisms of Protein-Processing Mechanoenzymes. Acs Omega. 8: 87-97
Torres-Delgado A, Kotamarthi HC, Sauer RT, et al. (2020) The intrinsically disordered N-terminal extension of the ClpS adaptor reprograms its partner AAA+ ClpAP protease. Journal of Molecular Biology
Kotamarthi HC, Sauer RT, Baker TA. (2020) The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation. Cell Reports. 30: 2644-2654.e3
Olivares AO, Kotamarthi HC, Stein BJ, et al. (2017) Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines. Proceedings of the National Academy of Sciences of the United States of America
Kotamarthi HC, Ainavarapu SRK. (2017) Mechanical Unfolding Studies on Single-Domain SUMO and Multi-Domain Periplasmic Binding Proteins Biophysical Reviews and Letters. 12: 1-10
Kotamarthi HC, Yadav A, Koti Ainavarapu SR. (2015) Small peptide binding stiffens the ubiquitin-like protein SUMO1. Biophysical Journal. 108: 360-7
Sarkar R, Kotamarthi H, Koti A, et al. (2015) Relative Mechanical Flexibility of Ubiquitin Family Proteins: A Study using Elastic Network Model Biophysical Journal. 108: 60a
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
Kotamarthi HC, Narayan S, Ainavarapu SRK. (2014) Mechanical unfolding of ribose binding protein and its comparison with other periplasmic binding proteins Journal of Physical Chemistry B. 118: 11449-11454
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