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Piyali Guhathakurta (Research associate)


My long-range goal is to understand the structure and dynamics of the actin-myosin interface during muscle contraction and to begin to apply this knowledge to the fight against heart diseases. Most current models of muscle contraction propose that force generation in the actomyosin ATPase cycle is associated with structural transitions in actin and myosin. However, these models are based on indirect structural data and speculative model-building, and they do not clearly define the structure of the actin-myosin interface and the structural rearrangements within this interface that are responsible for large decreases in the affinity of myosin for actin upon ATP binding to myosin. It is my hypothesis that changes in these specific contacts are crucial for understanding muscle function, and for understanding the molecular mechanism of some cardiomyopathies. We already developed cell culture systems for both actin and myosin that allowed me to place spectroscopic probes at desired sites of interest and introduced mutations that are known to cause human cardiomyopathy.  In Thomas Lab, I mainly use a pulsed laser and time-resolved fluorescence detection to measure distances between probes on actin and myosin by fluorescence resonance energy transfer. This will lay the groundwork not only for revising and clarifying these models, but also for investigating directly the mechanisms of diseases associated with the actin-myosin interaction

   I am mainly collaborating with Dr. Ewa Prochniewicz and Dr. Joe Muretta of Thomas Lab in this project.  I also had collaboration with Dr. Margaret Titus lab in University of Minnesota.



  1. The amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain. Piyali Guhathakurta, Ewa Prochniewicz and David D Thomas Proc Nat Acad Sci USA (2015) 112:4660-4665.
  2. The Structural Dynamics of Actin during Active Interaction with Myosin Depends on the Isoform of the Essential Light Chain. Ewa Prochniewicz, Piyali Guhathakurta and David D Thomas, Biochemistry (2013) 52:1622−1630.
  3. Allosteric communication in Dyctiostelium myosin II. Piyali Guhathakurta, Ewa Prochniewicz, Joseph M Muretta, MA Titus, and David D. Thomas. 2012. J Muscle Res Cell Motil 33:305-12.
  4. Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study, Piyali Guhathakurta, Debi Choudhury, Rakhi Dasgupta and J. K. Dattagupta, Biochemical and Biophysical Research Communication
  5. Structural basis of the unusual stability and substrate specificity of Ervatamin C, a plant cysteine protease from Ervatamia coronaria, Piyali Guhathakurta, Sampa Biswas, Chandana Chakrabarti, Monica Sundd, Medicherla V. Jagannadham and Jiban K. Dattagupta, Biochemistry
  6. Structure of diferric hen serum transferrin at 2.8Å resolution, Piyali Guhathakurta, Debi Choudhury, Rakhi Dasgupta and J. K. Dattagupta. Acta Cryst
  7. Crystallographic studies of an iron-transport protein explains the functional differences between two same gene products by Piyali Guhathakurta, Physics Teacher, Vol. 45,July-September (2003), 62-66.
  8. Purification and preliminary X-ray studies in hen sero transferrin in apo- and holo- forms, Debi Choudhury, Piyali Guhathakurta, Rakhi Dasgupta, U. Sen, S. Biswas, C. Chakrabarti and J. K. Dattagupta. Biochemical and Biophysical Research Communication
  9. Human specific insertion/deletion polymorphism in Indian populations and their possible evolutionary implications, Partha P Majumdar, Bidyut Roy, Sanat banerjee, Madan Chakrabarty, Badal Dey, Monami Roy, Piyali Guhathakurta  and Samir K Sil. European Journal of Human Genetics