Singularities ubiquitously exist in different fields and play a pivotal role in probing the fundamental laws of physics and developing highly sensitive sensors. Nevertheless, achieving higher-order (≥3) singularities, which exhibit superior performance, typically necessitates meticulous tuning of multiple (≥3) coupled degrees of freedom or additional introduction of nonlinear potential energies. Here we propose theoretically and confirm using mechanics experiments, the existence of an unexplored cusp singularity in the phase-tracked (PhT) steady states of a pair of coherently coupled mechanical modes without the need for multiple (≥3) coupled modes or nonlinear potential energies. By manipulating the PhT singularities in an electrostatically tunable micromechanical system, we demonstrate an enhanced cubic-root response to frequency perturbations. This study introduces a new phase-tracking method for studying interacting systems and sheds new light on building and engineering advanced singular devices with simple and well-controllable elements, with potential applications in precision metrology, portable nonreciprocal devices, and on-chip mechanical computing.
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http://dx.doi.org/10.1038/s41467-023-43708-y | DOI Listing |
Nat Commun
November 2020
Department of Anatomy and Structural Biology and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
Cytoplasmic dynein is the primary motor for microtubule minus-end-directed transport and is indispensable to eukaryotic cells. Although each motor domain of dynein contains three active AAA+ ATPases (AAA1, 3, and 4), only the functions of AAA1 and 3 are known. Here, we use single-molecule fluorescence and optical tweezers studies to elucidate the role of AAA4 in dynein's mechanochemical cycle.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
May 2015
Department of Anatomy and Structural Biology, Gruss Lipper Biophotonics Center, and
Cytoplasmic dynein is a homodimeric microtubule (MT) motor protein responsible for most MT minus-end-directed motility. Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellular activities) per motor domain (AAA1-4). The main site of ATP hydrolysis, AAA1, is the only site considered by most dynein motility models.
View Article and Find Full Text PDFNat Struct Mol Biol
January 2015
1] Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA. [2] Department of Physics, University of California, Berkeley, Berkeley, California, USA.
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