The proteins that make up all living things are alive with music. Just ask Markus Buehler: The musician and MIT professor develops artificial intelligence models to design new proteins, sometimes by translating them into sound. His goal is to create new biological materials for sustainable, non-toxic applications. In a project with the MIT-IBM Watson AI Lab, Buehler is searching for a protein to extend the shelf-life of perishable food. In a new study in Extreme Mechanics Letters, he and his colleagues offer a promising candidate: a silk protein made by honeybees for use in hive building.
In another recent study, in APL Bioengineering, he went a step further and used AI discover an entirely new protein. As both studies went to print, the Covid-19 outbreak was surging in the United States, and Buehler turned his attention to the spike protein of SARS-CoV-2, the appendage that makes the novel coronavirus so contagious. He and his colleagues are trying to unpack its vibrational properties through molecular-based sound spectra, which could hold one key to stopping the virus. Buehler recently sat down to discuss the art and science of his work… Continue reading.
The 20 amino acids that make up the building blocks of a protein contain chemical bonds that vibrate at different frequencies. Markus Buehler, a materials scientist and engineer at the Massachusetts Institute of Technology, coded that information, along with the intricate folding patterns of proteins, so that it could be represented as musical properties such as volume, speed and concurrent melodies (known in music theory as counterpoint).
The researchers then took their work a major step further. By feeding the musical interludes generated from known proteins into a neural network, the team trained the artificial intelligence system to develop novel variations of those rhythms—musical representations of proteins that did not yet exist… Continue reading.
Want to create a brand new type of protein that might have useful properties? No problem. Just hum a few bars.
In a surprising marriage of science and art, researchers at MIT have developed a system for converting the molecular structures of proteins, the basic building blocks of all living beings, into audible sound that resembles musical passages. Then, reversing the process, they can introduce some variations into the music and convert it back into new proteins never before seen in nature.
Although it’s not quite as simple as humming a new protein into existence, the new system comes close. It provides a systematic way of translating a protein’s sequence of amino acids into a musical sequence, using the physical properties of the molecules to determine the sounds. Although the sounds are transposed in order to bring them within the audible range for humans, the tones and their relationships are based on the actual vibrational frequencies of each amino acid molecule itself, computed using theories from quantum chemistry… Continue reading.
Spider silk, already known as one of the strongest materials for its weight, turns out to have another unusual property that might lead to new kinds of artificial muscles or robotic actuators, researchers have found.
The resilient fibers, the team discovered, respond very strongly to changes in humidity. Above a certain level of relative humidity in the air, they suddenly contract and twist, exerting enough force to potentially be competitive with other materials being explored as actuators — devices that move to perform some activity such as controlling a valve.
The findings are being reported today in the journal Science Advances, in a paper by MIT Professor Markus Buehler, head of the Department of Civil and Environmental Engineering, along with former postdoc Anna Tarakanova and undergraduate student Claire Hsu at MIT; Dabiao Liu, an associate professor at Huazhong University of Science and Technology in Wuhan, China; and six others… Continue reading.
The stretchiness that allows living tissues to expand, contract, stretch, and bend throughout a lifetime is the result of a protein molecule called tropoelastin. Remarkably, this molecule can be stretched to eight times its length and always returns back to its original size.
Now, for the first time, researchers have decoded the molecular structure of this complex molecule, as well as the details of what can go wrong with its structure in various genetically driven diseases.
Tropoelastin is the precursor molecule of elastin, which along with structures called microfibrils is the key to flexibility of tissues including skin, lungs, and blood vessels. But the molecule is complex, made up of 698 amino acids in sequence and filled with disordered regions, so unravelling its structure has been a major challenge for science… Continue reading.
“Two-dimensional materials” — materials deposited in layers that are only a few atoms thick — are promising for both high-performance electronics and flexible, transparent electronics that could be layered onto physical surfaces to make computing ubiquitous.
The best-known 2-D material is graphene, which is a form of carbon, but recently researchers have been investigating other 2-D materials, such as molybdenum disulfide, which have their own, distinct advantages.
Producing useful electronics, however, requires integrating multiple 2-D materials in the same plane, which is a tough challenge. In 2015, researchers at King Abdullah University in Saudi Arabia developed a technique for depositing molybdenum disulfide (MoS2) next to tungsten diselenide (WSe2), with a very clean junction between the two materials. With a variation of the technique, researchers at Cornell University then found that they could induce long, straight wires of MoS2 — only a few atoms in diameter— to extend into the WSe2, while preserving the clean junction.
The researchers contacted Markus Buehler, the McAfee Professor of Engineering in MIT’s Department of Civil and Environmental Engineering, who specializes in atomic-level models of crack propagation, to see if his group could help explain this strange phenomenon… Continue reading.
When it comes to concocting the complex mix of molecules that makes up fibers of natural silk, nature beats human engineering hands down. Despite efforts to synthesize the material, artificial varieties still cannot match the natural fiber’s strength.
But by starting with silk produced by silkworms, breaking it down chemically, and then reassembling it, engineers have found they can make a material that is more than twice as stiff as its natural counterpart and can be shaped into complex structures such as meshes and lattices.
The new material is dubbed regenerated silk fiber (RSF) and could find a host of applications in commercial and biomedical settings, the researchers say. The findings are reported in the journal Nature Communications, in a paper by McAfee Professor of Engineering Markus Buehler, postdoc Shengjie Ling, research scientist Zhao Qin, and three others at Tufts University… Continue reading.
WASHINGTON, D.C.— The American Institute for Medical and Biological Engineering (AIMBE) has announced the pending induction of Markus J. Buehler, Ph.D., Professor & Department Head, Civil and Environmental Engineering, Massachusetts Institute of Technology, to its College of Fellows. Dr. Buehler was nominated, reviewed, and elected by peers and members of the College of Fellows For applying computational tools to elucidate complex biomaterials behavior, design new biomaterials, and integrating experiment and simulation across multiple scales.