Journal article
Eric R. Kuhn, A. Naik, Brianne E. Lewis, Keith M. Kokotovich, Meishan Li, Timothy L. Stemmler, L. Larsson, B. Jena
Nano letters (Print), 2018
Nano letters (Print), 2018
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APA
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Kuhn, E. R., Naik, A., Lewis, B. E., Kokotovich, K. M., Li, M., Stemmler, T. L., … Jena, B. (2018). Nanothermometry Reveals Calcium-Induced Remodeling of Myosin. Nano Letters (Print).
Chicago/Turabian
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Kuhn, Eric R., A. Naik, Brianne E. Lewis, Keith M. Kokotovich, Meishan Li, Timothy L. Stemmler, L. Larsson, and B. Jena. “Nanothermometry Reveals Calcium-Induced Remodeling of Myosin.” Nano letters (Print) (2018).
MLA
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Kuhn, Eric R., et al. “Nanothermometry Reveals Calcium-Induced Remodeling of Myosin.” Nano Letters (Print), 2018.
BibTeX Click to copy
@article{eric2018a,
title = {Nanothermometry Reveals Calcium-Induced Remodeling of Myosin.},
year = {2018},
journal = {Nano letters (Print)},
author = {Kuhn, Eric R. and Naik, A. and Lewis, Brianne E. and Kokotovich, Keith M. and Li, Meishan and Stemmler, Timothy L. and Larsson, L. and Jena, B.}
}
Abstract
Ions greatly influence protein structure-function and are critical to health and disease. A 10, 000-fold higher calcium in the sarcoplasmic reticulum (SR) of muscle suggests elevated calcium levels near active calcium channels at the SR membrane and the impact of localized high calcium on the structure-function of the motor protein myosin. In the current study, combined quantum dot (QD)-based nanothermometry and circular dichroism (CD) spectroscopy enabled detection of previously unknown enthalpy changes and associated structural remodeling of myosin, impacting its function following exposure to elevated calcium. Cadmium telluride QDs adhere to myosin, function as thermal sensors, and reveal that exposure of myosin to calcium is exothermic, resulting in lowering of enthalpy, a decrease in alpha helical content measured using CD spectroscopy, and the consequent increase in motor efficiency. Isolated muscle fibers subjected to elevated levels of calcium further demonstrate fiber lengthening and decreased motility of actin filaments on myosin-functionalized substrates. Our results, in addition to providing new insights into our understanding of muscle structure-function, establish a novel approach to understand the enthalpy of protein-ion interactions and the accompanying structural changes that may occur within the protein molecule.
