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. 2025 Aug 15;18(3):571–576. doi: 10.1007/s12551-025-01354-2

Remembering Roger Cooke (1940–2024): his life and science

Nariman Naber 1,✉
PMCID: PMC13486421  PMID: 42621062

Roger Cooke, a biophysicist, visionary and a creative thinker, died on August 1st, 2024, at the age of 84. His work in the biophysics and physiology of motor proteins is pivotal to understanding the molecular mechanisms by which these proteins generate force. The discovery of the super relaxed state opened a new field in the study of skeletal and cardiac muscle. Due to this advancement, it made way for developing new treatments for human disease. And I had the privilege of working directly with him for 35 years.

Early years

Roger was born in Ann Arbor, Michigan, on February 22nd, 1940, a birth date that he shared with the great first president of the United States, George Washington. He grew up in Lexington, Kentucky. It was at the early age of 12 when Roger decided to go into science. By the time he turned 18, he was doing research in the physiology lab of Professor Louis Boyarsky at the University of Kentucky. During the summer, he fulfilled his duties as a young, southern boy by working in the tobacco fields, hanging tobacco in tall and dangerous barns. One day, he fell unconscious from a severe fall and was taken to the farmhouse, where a bucket of cold water was dumped on his head. Five minutes later, he was back to work. I guess the bucket of water was the neurological ICU in Kentucky in the 1950s.

Roger was an avid swimmer. He won the Kentucky state championship in the 50-yard freestyle. After graduating from high school, he headed north to MIT. Here, he got his undergraduate degree in Physics in 1962, and he was part of the MIT swim team throughout his college career. While his pursuits as an over-achiever landed him in great standing with his professors and classmates, he was also a bit of a class clown, iconically placing a randomly discovered toilet in the halls of MIT at the top of the MIT dome. This is what truly sealed his legacy at MIT, making headlines across campus the next day.

After MIT, Roger headed Midwest to the University of Illinois where he worked for Dr. Hans Fraunfelder. Here, he developed an interest in the application of Physics to Biology, eventually earning his PhD in Physics in 1968 (Cooke et al. 1968).

Heading further west, he arrived in San Francisco in the winter of 1968. Only 6 months after the infamous “summer of love,” which he always complained about missing dearly, he began his postdoctoral research at UCSF under the supervision of Dr. Manuel Morales at the Cardiovascular Research Institute. Dr. Morales was a Physicist/Mathematician who interpreted and studied muscle as a biological machine, which sparked Roger’s interest to further research this area of study (Cooke and Morales 1969, 1971; Quinlivan et al. 1969).

Roger joined the faculty at UCSF in 1971. The rest is history. After his official retirement in 2009, he continued to work in the lab until recently. Roger was one of the longest-standing faculty members in the Department of Biochemistry and Biophysics and The Cardiovascular Research Institute at UCSF.

Roger’s contribution to science

Roger Cooke’s career in science spanned over 60 years, focusing on the biophysics and physiology of motor proteins, in muscle and non-muscle tissues. These proteins play a role in numerous biological processes, including muscle contraction, cell division and the movement of intracellular organelles. The Cooke lab studied the mechanism of action of two classes of motor proteins, the myosin family and the kinesin family, which share a structural homology. The central long-range goal of the lab was to understand the molecular mechanisms by which these two classes of motor proteins generate force.

The interaction of the two proteins, actin and myosin, produces the force of muscle contraction and is also involved in the motility of all eukaryotic cells. Electron paramagnetic resonance (EPR) spectroscopy and fluorescence spectroscopy were used to measure the orientation, conformation, and dynamics of both actin and myosin in active muscle fibers. In the early 1970 s, the established model for myosin’s mechanism of force generation was known as the rowing oar model. In this model, myosin acted as a rigid structure that alters its orientation to generate force and motion. In collaboration with Dr. Dave Thomas, this model was tested using spin-probes to measure orientation (Thomas and Cooke 1980; Cooke et al. 1982a, 1984; Cooke 1986). It was surprising to discover that the region of the myosin head that was monitored by the spin probe did not “row”. These data along with data from other investigators led to a new model of myosin’s action, in which a portion of myosin bound tightly and rigidly to actin while another portion, called the lever arm, changed orientation to produce force and motility. This model rapidly became the established model for myosin’s mechanism of developing force and motion (Fig. 1).

Fig. 1.

Fig. 1

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Kinetic model of myosin head rotation proposed by Roger Cooke and David Thomas in 1982 (Cooke et al. 1982a). This model shows the two-step rotation of myosin head when bound to actin, effectively functioning as a flexible lever on actin. A The catalytic domain of myosin (CD) undergoes disorder-to-order transition resulting in a 5- nm shift in actin. B Next, actin is further propelled by another 5 nm due to the rotation of the light chain domain (LCD) on the flexible head of myosin

Kinesin motors are smaller than myosin but generate forces and displacements that are similar. Electron paramagnetic resonance spectroscopy was used to monitor conformational changes in these motors. Paramagnetic probes (“spin labels”) were placed on selected active elements. The data from these probes showed how the neck-linker docked and undocked to the motor domain in response to binding to ATP or microtubules (Naber et al. 2003a, b; Rice et al. 1999; Sindelar et al. 2002). This led directly to the neck-linker docking model of kinesin motility. Further work with spin probes examined the energetics of this process and the role of the neck linker as an entropic spring. This model has now become the established paradigm for how kinesin and some other motors produce force and motion (Rice et al. 2003; Sindelar et al. 2002). This work was carried out in collaboration with the laboratories of Dr. Ron Vale and Dr. Robert Fletterick.

For several decades, the Cooke lab also investigated the mechanics of skinned muscle fibers to explore the mechanisms of muscle fatigue and better understand how muscle fibers adapt to intense activity and fatigue (Karatzaferi et al. 2003, 2008; Cooke 2007; Myburgh and Cooke 1997; Pate et al. 1995; Cooke et al. 1988; Cooke and Pate 1985; Pate and Cooke 1989). In collaboration with the late Dr. Edward Pate, Dr. Cooke developed an apparatus capable of measuring the forces, velocities, and stiffness of single skinned muscle fibers. The fiber membrane was removed, allowing investigators to perfuse the myofibrils with various solutions. These studies showed that the accumulation of several metabolic products in the interior of the muscle cell could account for some of the fatigue experienced by long-distance runners, though it did not explain all of it. A subunit of myosin becomes phosphorylated during heavy use, and this myosin phosphorylation works synergistically with metabolite accumulation to inhibit fiber shortening velocity (Persechini et al. 1985; Franks et al. 1984; Cooke et al. 1982b; Stull et al. 1980). These results laid the groundwork for a field that continues to be actively investigated. The collaboration with Dr. Pate lasted over 30 years and resulted in 51 publications.

Dr. Cook’s most notable scientific achievements came after his official retirement in 2009. The morning after his retirement, he returned to the lab and started working at the bench doing experiments. Roger discovered a new state of skeletal muscle myosin, which has a highly inhibited ATPase activity, called the super-relaxed state (SRX) (Stewart et al. 2010). The SRX is in equilibrium with a disordered relaxed state of myosin, the disordered relaxed state (DRX), which has a higher ATPase activity. SRX was visualized by performing single nucleotide turnovers in skinned muscle fibers using a fluorescent analogue of ATP (mant-ATP) and chasing it with ATP. The difference in energy consumption between the SRX and DRX provides an entirely new method for modulating the rate at which calories are burned, impacting obesity and type 2 diabetes (Nogara et al. 2016a, b; Cooke 2011). Observations of the metabolic rate of relaxed skeletal muscle in vivo indicate that the SRX is the physiologically dominant state, leading to the energy economy of relaxed muscle. Pharmaceuticals that can destabilize the SRX and populate the DRX could increase the whole-body metabolic rate by 1000 Cal/day, potentially offering more effective therapies for obesity and type 2 diabetes. Muscle is an excellent target for increased thermogenesis, due to its large reserve metabolic capacity. Therefore, the discovery of the SRX has significant implications for developing new treatments for obesity and type 2 diabetes.

Due to the importance of this state for developing new treatments for human disease, the lab’s efforts concentrated on the SRX. We discovered fluorescent probes that can be used to monitor the population of the super-relaxed state. These probes were used to carry out high-throughput screens to find compounds that can alter the population of this state in skeletal muscle to treat human diseases. Screening 2128 compounds identified one that destabilized the SRX in fast-twitch muscle myosin and increased the ATPase activity of relaxed fibers. The compound, piperine, an alkaloid found in black pepper, was characterized in a series of in vitro experiments (Nogara et al. 2016a). Piperine increased the ATPase activity of skinned muscle fibers, with a dissociation constant Kd in the ATPase assay of ~ 2 μM. It was effective in fast skeletal muscle, affecting relaxation but not contraction, and had no effect on cardiac muscle (Nogara et al. 2016a). This work landed us a front-page cover in The Proceedings of the National Academy of Sciences journal (PNAS), opening a new field in the study of striated muscle. A later search of the literature showed that piperine mitigates both obesity and type 2 diabetes at very high doses in rodents (BrahmaNaidu et al. 2014; Okumura et al. 2010; Choi et al. 2013). Though the mechanism for this effect was not identified. Roger proposed that the mechanism is its effect on the SRX. Piperine is also reported to affect several other targets, including liver enzymes and trans-membrane channels. It is small, too hydrophobic, and binds to too many targets to make a good therapeutic compound in humans. Thus, while piperine itself may not function effectively as a therapeutic in humans, it could serve as a lead compound for developing similar molecules with therapeutic potential.

This approach was extended to cardiac muscle, revealing that the cardiac super-relaxed state has different properties compared to the skeletal super-relaxed state. In skeletal fibers, the super-relaxed state modulates the resting metabolic rate. In cardiac cells, the SRX is involved in modulating the contractility of the myocardium. This modulation may occur via phosphorylation of myosin and myosin-binding protein C (MBP-C). In collaboration with Dr. Cris dos Remedios, we found that ablation of the protein myosin binding protein C destabilizes the super-relaxed state in permeable cardiac tissue (McNamara et al. 2016). We also found that mutations in the myosin binding protein C also destabilize the super-relaxed state. This destabilization causes the hyperactivation of cardiac muscle, leading to hypertrophic cardiomyopathy (McNamara et al. 2017). The exciting aspect of this new state is that manipulating it can provide therapies to treat human cardiac diseases. Agents that alter the stability of the SRX in cardiac cells could be used to modulate the contractility of the myocardium, providing effective treatments for many cardiac disorders, including heart failure and cardiomyopathies. In collaboration with Dr. Jim Spudich’s laboratory and with MyoKardia, we have discovered small molecules that can stabilize the super-relaxed state, leading to a reduction in the contractility of cardiac tissue (Anderson et al. 2018). These molecules are now in clinical trials for the treatment of hypertrophic cardiomyopathies. This work has opened up a new field in the study of cardiac muscle.

Most recently, a construct was made consisting of two regulatory light chains (RLC), along with the fragment of the heavy chain to which they bind and a portion of the coiled-coil rod, sufficient to form a dimer. Together these form a mini fragment of myosin, which we call the regulatory domain. This domain is important, because one of the interfaces stabilizing the SRX is formed between the two RLCs. We have shown that piperine binds to this mini-fragment and changes its conformation (Tolkatchev et al. 2018). This work was done in collaboration with Dr. Alla Kostyukova at Washington State University.

2022 Biophysical Society Fellow award

Roger was an active member of the Biophysical Society. He was elected as a Fellow of the Biophysical Society for his lifetime contributions to the field of Biophysics, particularly for his landmark discoveries in motor proteins, which defined (a) the current lever-arm mechanisms in myosin and its “super-relaxed” state, and (b) the mechanism, structure, and energetics of the kinesin motors. This award is given to Society members who have demonstrated sustained excellence in science and have contributed to the expansion of the field of Biophysics.

Barnyard engineering

Roger possessed a multitude of talents and a broad range of abilities. He had several drawers full of tools in the lab that he used to build equipment, saving the lab thousands of dollars over the years. There are many stories to share in this regard. In the late 1970 s and early 1980 s, he managed to build his own tensiometer (measuring molecular forces), which cost him $5000 to make and saved the lab $55,000 compared to purchasing one. Throughout his career, he helped at least two other labs build their own tensiometers, saving them thousands of dollars as well.

On another occasion, we needed to conduct an EPR experiment on fibers at lower temperatures, which required a cooling system. We contacted Bruker, and they quoted us a price tag of $17,000. Roger walked to the hardware store down the street, bought a few items, and assembled a cooling system that cost the lab only $265.

My personal favorite of the many inventions he self-engineered was a small flow cell for measuring the super-relaxed state of single muscle fibers. The cost was about $0. It was made from a glass slide, two coverslips, and a touch of glue.

Roger was versatile, resourceful, and accomplished—a true jack-of-all-trades whose talents influenced and enhanced the work of many labs.

Roger the athlete

Roger was an avid sports enthusiast throughout his lifetime. He was a competitive swimmer, abalone diver, surfer, skier, and freehand rock climber. As a competitive swimmer, he consistently surpassed any 20-something-year-old graduate student or post-doc who tried to challenge him, often frustrating the younger generation on campus. Roger also completed the Alcatraz swim three times, a two-mile stretch in the San Francisco Bay from Alcatraz to Fisherman’s Wharf at a temperature of 55°F. Mind you, he accomplished these feats after the age of 60.

On the Parnassus campus, he refused to take the elevator, climbing 11 stories of stairs just to get to the lab three times a day. He also ran the Bay to Breakers 35 times, and if, for any reason, he could not run it, he would walk the full 7.5 miles. However, his greatest love of all was sailing. Roger would take any opportunity to entertain everyone on his boat and share his love of sailing with them. He completed sails far and wide, spanning global regions from The Bahamas to Greece to Australia. Most impressively, he satisfied his adventurous spirit between experiments, perfectly balancing life and science.

The human side of Roger

Roger set the gold standard not only on a scientific level but, more importantly, on a human level. I can share many stories of Roger’s humanity prevailing across various circumstances; however, there is not enough space in this memory book to do so. He was a great person and a close friend who was incredibly kind. He was always able to see the world in a different and positive way, making remarks that were refreshing, original, witty, and funny.

Having worked with Roger for many years, I can attest to his great character, modesty, humility, and deep respect for every person he interacted with daily. Roger was humble and inspiring. His work-life balance was impressive and set an inspirational standard for all those who knew him. Working for Roger was a fun, amazing experience and a tremendous opportunity. He was patient, always pleasant, and a joy to work with every single day over the course of my 35 years in his lab.

Roger loved his science so much that in his final year, he temporarily lost his speech for two days. Upon regaining his speech, the first word that came out of his mouth was “myosin”.

One of his famous quotes used in the face of any challenge was, “for every problem, there is a solution.”

There's nothing more beautiful than a life fully lived. Your journey has ended, but our love for you will never fade. Rest in peace Roger.

Roger Cooke and Nariman Naber, May 17th, 2017

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Acknowledgements

I would like to thank Professor David Thomas for editing and providing suggestions to the original version of this manuscript. Thanks to Dr. Amy Li for her assistance with this manuscript. Figure 1 was adapted from his presentation at Roger’s memorial held at UCSF in 2024.

Author contribution

This commentary is written by one author, Dr. Nariman Naber in remembrance of the late Dr. Roger Cooke.

Data availability

No datasets were generated or analysed during the current study.

Declarations

Competing interests

The author declares no competing interests.

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Associated Data

This section collects any data citations, data availability statements, or supplementary materials included in this article.

Data Availability Statement

No datasets were generated or analysed during the current study.

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