Shane Nelson
Assistant Professor, Molecular Physiology & Biophysics
Health Science Research Facility, 115
149 Beaumont Avenue
Burlington, VT 05405
United States
- Ph.D., University of Wyoming
Department of Molecular Physiology & Biophysics
Areas of expertise
single-molecule biophysics and molecular motor proteins.
BIO
Dr Nelson received his Ph.D. in Molecular Biology at the University of Wyoming in 2006, where he developed a novel recombinant biomaterial based on major ampullate spider silk proteins, combining molecular dynamics simulations with molecular biology. For his post-doctoral studies, Dr. Nelson pursued his interest in molecular motors and single-molecule biophysics in the laboratory of Dr. David Warshaw, at the University of Vermont. Dr. Nelson joined the faculty in the Department of Molecular Physiology and Biophysics at the University of Vermont in 2016 as a faculty scientist and was promoted to an independent position as assistant professor in 2025.
The Nelson Lab combines state-of-the-art single-molecule imaging, optical trapping, mathematical modeling and other biophysical approaches to investigate the structure, dynamics, and function of myosin and other molecular motor proteins in health and disease.
Muscle contraction is powered by myosin, a double-headed molecular motor that generates force and movement through hydrolysis of ATP. Normally, myosin exists in a dynamic equilibrium between two functional states: the Disordered Relaxed (DRX) state, which is available for force generation, and the Super-Relaxed (SRX) state, an autoinhibited, energy-conserving state that is thought to serve as a reserve pool of motors that can be recruited in response to physiological demand.
The structural basis of the SRX state is widely believed to involve the interacting-heads motif (IHM), an asymmetric folded conformation of the myosin heads. Importantly, disruptions in the balance between SRX and DRX populations have been linked to numerous skeletal and cardiac muscle disorders, highlighting this regulatory mechanism as a promising therapeutic target.
Despite its significance, the molecular basis and regulation of the SRX and DRX states remains the subject of intense debate. To address these questions, the Nelson Lab has developed innovative single-molecule methodologies that simultaneously monitor myosin’s structural and functional states while directly measuring transitions between them. These approaches provide unprecedented insight into the mechanisms that regulate muscle contractility and their roles in human disease.
Publications
Bio
Dr Nelson received his Ph.D. in Molecular Biology at the University of Wyoming in 2006, where he developed a novel recombinant biomaterial based on major ampullate spider silk proteins, combining molecular dynamics simulations with molecular biology. For his post-doctoral studies, Dr. Nelson pursued his interest in molecular motors and single-molecule biophysics in the laboratory of Dr. David Warshaw, at the University of Vermont. Dr. Nelson joined the faculty in the Department of Molecular Physiology and Biophysics at the University of Vermont in 2016 as a faculty scientist and was promoted to an independent position as assistant professor in 2025.
The Nelson Lab combines state-of-the-art single-molecule imaging, optical trapping, mathematical modeling and other biophysical approaches to investigate the structure, dynamics, and function of myosin and other molecular motor proteins in health and disease.
Muscle contraction is powered by myosin, a double-headed molecular motor that generates force and movement through hydrolysis of ATP. Normally, myosin exists in a dynamic equilibrium between two functional states: the Disordered Relaxed (DRX) state, which is available for force generation, and the Super-Relaxed (SRX) state, an autoinhibited, energy-conserving state that is thought to serve as a reserve pool of motors that can be recruited in response to physiological demand.
The structural basis of the SRX state is widely believed to involve the interacting-heads motif (IHM), an asymmetric folded conformation of the myosin heads. Importantly, disruptions in the balance between SRX and DRX populations have been linked to numerous skeletal and cardiac muscle disorders, highlighting this regulatory mechanism as a promising therapeutic target.
Despite its significance, the molecular basis and regulation of the SRX and DRX states remains the subject of intense debate. To address these questions, the Nelson Lab has developed innovative single-molecule methodologies that simultaneously monitor myosin’s structural and functional states while directly measuring transitions between them. These approaches provide unprecedented insight into the mechanisms that regulate muscle contractility and their roles in human disease.