Dr. Gladys W. Royal...

Dr. Gladys Royal (left), Dr. W. E. Reed (left center), R. L. Satoera (right center) and Dr. George Royal (right), with x-ray equipment, North Carolina A&T College, 1961

By THE AGRICULTURAL AND TECHNICAL, COLLEGE, GREENSBORO, N. C. - THE A&T COLLEGE REGISTER, VOLUME XXXII, No. 8 , FRIDAY, JANUARY 13, 1961, Public Domain, https://commons.wikimedia.org/w/index.php?curid=42353373

Topics: African Americans, Diversity in Science, Biochemistry, Nanotechnology, Women in Science

See: Biochemistry and structural DNA nanotechnology: an evolving symbiotic relationship.

Gladys W. Royal (August 29, 1926 – November 9, 2002) is one of a small number of early African-American biochemists. Part of one of the few African-American husband-and-wife teams in science, Gladys worked with George C. Royal on research supported by the United States Atomic Energy Commission. She later worked for many years as principal biochemist at the Cooperative State Research Service of the U.S. Department of Agriculture. Royal was also active in the civil rights movement in Greensboro, North Carolina.

Royal was born Gladys Geraldine Williams on August 29, 1926, in Dallas, Texas. She graduated from Dillard University with a B.Sc. at the age of 18 in 1944. She married George C. Royal in 1947.

Royal accompanied her husband to Tuskegee, Alabama, where he taught microbiology in 1947-1948, to Ohio State University and Ohio Agricultural Experiment Station, where he was a research assistant from 1948 to 1952, and to North Carolina Agricultural and Technical College in Greensboro where he became an assistant professor of Bacteriology in 1952. At Tuskegee and Ohio State she took classes; by 1953, she was sufficiently qualified to become a professor of chemistry at North Carolina Agricultural and Technical College in Greensboro.

In 1954, Royal received her M.Sc. in organic chemistry from Tuskegee. She had also taken classes at the University of Wisconsin and at Ohio State University, from which she received her Ph.D. in 1954. Her thesis, The Influence of Rations Containing Sodium Acetate and Sodium Propionate on the Composition of Tissues From Feeder Lambs, involved experimental work in flavor chemistry, testing the effects of various feed regimens on the taste of meat.

In the late 1950s and early 1960s, the Royals collaborated on important research including that funded by the United States Atomic Energy Commission involving bone marrow transplants to treat radiation overdoses. Their work had direct relevance to cancer treatment, which used high doses of radiation and could cause tissue damage. It also reflected Cold war fears of possible nuclear attack.

African-American husband-and-wife teams in science were extremely rare in the early and mid-20th century due to the social, educational and economic climate regarding African Americans in the United States.

The Royals had six children: George Calvin Royal III, Geraldine Gynnette Royal, Guericke Christopher Royal, jazz musician Gregory Charles Royal, Michelle Renee McNear, and Eric Marcus Royal.

Source: Wikipedia/Gladys_W._Royal

Electroceuticals...

Image Source: Eureka Alert! AAAS

Topics: Biology, Biochemistry, Bioengineering, Biomedicine

Light-induced processes at the interface between silicon-based structures and biological ones can be used to remotely control a wide range of biological activities – from single cell calcium signalling to brain activity – without any genetic engineering of the biological systems involved. The new finding could help in the development of “electroceuticals”, in which bioelectric signals could be modulated to treat disease. As well as biomedical applications, the toolkits employed could also be used to study fundamental biophysical processes.

Silicon-based materials are widely used in biological applications. Two examples include silicon nanowire-based transistors for electrically monitoring the signals in cardiomyocytes and bioelectronics implants for the heart. They are rarely found in remotely controlled and interconnect-free device set ups, however. This is because researchers do not fully understand the complex physicochemical processes at play at the interfaces between silicon and biological materials.

Remotely-controlled silicon structures could help treat disease, Belle Dumé, Nanotechweb.org

Clams and Biofuel...

Penn researchers are collaborating to study how giant clams convert sunlight into energy, which could lead to more efficient production of biofuel. Photo credit: Malcolm Browne

Topics: Biochemistry, Green Energy, Materials Science, Nanotechnology, Physics, Solar Power

Alison Sweeney of the University of Pennsylvania has been studying giant clams since she was a postdoctoral fellow at the University of California, Santa Barbara. These large mollusks, which anchor themselves to coral reefs in the tropical waters of the Indian and Pacific oceans, can grow to up to three-feet long and weigh hundreds of pounds. But their size isn’t the only thing that makes them unique.​​​​​​​​​​​​​​Anyone who has ever gone snorkeling in Australia or the western tropical Pacific Ocean, Sweeney says, may have noticed that the surfaces of giant clams are iridescent, appearing to sparkle before the naked eye. The lustrous cells on the surface of the clam scatter bright sunlight, which typically runs the risk of causing fatal damage to the cell, but the clams efficiently convert the sunlight into fuel. Using what they learn from these giant clams, the researchers hope to improve the process of producing biofuel.

​​​​​​​Sweeney, an assistant professor of physics in the Penn School of Arts and Sciences, and her collaborator Shu Yang, a professor of materials science and engineering in the School of Engineering and Applied Science, refer to the clams as “solar transformers” because they are capable of absorbing bright sunlight at a very high rate and scattering it over a large surface area. When the light is distributed evenly among the thick layer of algae living inside the clam, the algae quickly converts the light into energy.

“What those sparkly cells are doing,” Sweeney says, “is causing light to propagate very deeply into the clam tissue and spread out.”

“What those sparkly cells are doing,” Sweeney says, “is causing light to propagate very deeply into the clam tissue and spread out.”

After coming across Sweeney’s work, Yang struck up a collaboration to see if they could mimic the system by abstracting the principles of the clam’s process to create a material that works similarly. She and Ph.D. student Hye-Na Kim devised a method of synthesizing nanoparticles and adding them to an emulsion — a mixture of water, oil, and soapy molecules called surfactants — to form microbeads mimicking the iridocytes, the cells in giant clams responsible for solar transforming. Their paper has been published in Advanced Materials.

Penn Researchers Working to Mimic Giant Clams to Enhance the Production of Biofuel
Ali Sundermier, Evan Lerner, University of Pennsylvania News

Breadcrumbs and Evolution...

Schematic of the sandwich tunnelling electrode structure functionalized with RGD peptide, with a human integrin &alpha_Vβ₃ protein in the junction gap. Courtesy of Nano Futures.

Topics: Biology, Biochemistry, Chemistry, Nanotechnology

When electrochemistry, transient charging and heating effects all failed to explain the fluctuating high conductance detected in a human integrin protein, Stuart Lindsay at Arizona State University and his colleagues considered the possibility that the protein’s electronic properties teetered at a critical point between conducting and insulating states. Further analysis of the results revealed characteristics typical of a quantum critical point. While as yet unconfirmed, it is possible this "Goldilocks zone" may aid the protein’s functions, so that evolutionary advantages would have promoted the prevalence of this statistically unlikely electronic behaviour. On a more pragmatic level, the distinctive electronic signal is clearly identified against noisy backgrounds, and may have applications in single-molecule detection.

"There has long been this breadcrumb trail of evidence that proteins behave unusually electronically," explains Lindsay, director of the Biodesign Center for Single Molecule Biophysics at Arizona State University. "All the experiments you can shoot down because you don’t know the state of the protein or how many proteins you have there – here, for the first time, we trap a single protein in a well defined gap and in a condition in which the protein is native."

Lindsay worked alongside researchers at Arizona State University in the US and Eötvös Loránd University in Hungary to characterize the proteins both using a scanning tunnelling microscope (STM) similar to other groups, as well as with a "fixed-gap device" junction developed in work on DNA sequencing. Characterizing proteins by STM raises several issues because the precise chemistry and geometry of the STM tip are not known, and the native environment of these proteins differs greatly from a vacuum, where the physics is well established. However, Lindsay and his colleagues found that their less error-prone fixed-gap device also gave conductances several orders of magnitude greater than expected, and that they fluctuated.

Unexplained huge protein conductances hint at evolution, Anna Demming, Nanotechweb.org

Intrinsic Disorder...

Ricardo Bessa for Quanta Magazine

Topics: Biology, Biochemistry, Biophysics, Research

Proteins work like rigid keys to activate cellular functions — or so everyone thought. Scientists are discovering a huge number of proteins that shape-shift to do their work, upending a century-old maxim of biology.

Structure equals function: If there’s one thing we all learned about proteins in high school biology, that would be it. According to the textbook story of the cell, a protein’s three-dimensional shape determines what it does — drive chemical reactions, pass signals up and down the cell’s information superhighway, or maybe hang molecular tags onto DNA. For more than a century, biologists have thought that the proteins carrying out these functions are like rigid cogs in the cell’s machinery.

Of course, exceptions would occasionally crop up. A scientist might bump into a protein that performed its functions perfectly well yet didn’t have rigid structures. Most researchers chalked these cases up to experimental error, or dismissed them as insignificant outliers.

More recently, however, biologists have begun paying attention to these shapeshifters. Their findings are tearing down the structure-function dogma.

Proteins are chains of strung-together amino acids, and recent studies estimate that up to half of the total amino acid sequence that makes up proteins in humans doesn’t fold into a distinct shape. (While some of the proteins that make up this total are unstructured from end to end, others contain long unstructured regions side-by-side with structured ones.) “Partly, people didn’t realize how big that number was, and that’s why they ignored it,” said Julie Forman-Kay, a biochemist at the Hospital for Sick Children and the University of Toronto. “And partly they just didn’t know what to think of it.”

This fluidity — dubbed “intrinsic disorder” — endows proteins with a set of superpowers that structured proteins don’t have. Folded proteins tend to bind to their targets firmly, like a key in a lock, at just one or two spots, but their more stretched-out wiggly cousins are like molecular Velcro, attaching lightly at multiple locations and releasing with ease. This quick-on-quick-off binding’s effect in the cell is huge: It allows intrinsically disordered proteins — or IDPs, for short — to receive and respond to a slew of molecular messages simultaneously or in rapid succession, essentially positioning them to serve as cellular messaging hubs, integrating these multiple signals and switching them on and off in response to changes in the cell’s environment and to keep cellular processes ticking along as they should.

Quanta Magazine: The Shape-Shifting Army Inside Your Cells
Alla Katsnelson

Nitrogen-Doped Carbon...

Phenol-urea-formaldehyde (PUF) organic foam were used as precusors for the new monolithic nitrogen-containing microporous cellular activated carbons production. Carbonization and CO2 activation were used to prepare this novel monolithic nitrogen-containing activated carbon foam with both interconnected macroporous and micro/meso- porosity structures from the developed PUF organic foam. The macroporosity corresponded to the connected network of cells with diameters ranging from 100 to 600 µm, and the pinholes in the cell walls had diameters ranging from 1 to 2 µm. The micro/mesoporosity is located at the inner surface of the cells. They can be used just like the classic activated carbon as an adsorbent, catalyst support, energy storage and biological material in various industries, but higher adsorption kinetics. Credit: World Scientific Publishing

Topics: Biology, Biochemistry, Biotechnology, Research

Researchers have developed monolithic, nitrogen-containing, microporous, cellular-activated carbon from phenol-urea-formaldehyde (PUF) organic foam for CO2 and H2 adsorption. The macroporosity corresponded to the connected network of cells with diameters ranging from 100 to 600 μm, and the pinholes in the cell walls had diameters ranging from 1 to 2 μm. The micro/mesoporosity is located at the inner surface of the cells.

Phys.org: Researchers produced nitrogen-doped, cellular-structure-activated carbon

More information: Weigang Zhao et al, Preparation and Characterization of Nitrogen-Containing Cellular Activated Carbon for CO and H Adsorption, Nano (2016). DOI: 10.1142/S1793292017500072

Dr. Gerty Theresa Cori, née Radnitz...

Image Source: NobelPrize.org

Topics: Biochemistry, Diversity, Diversity in Science, Metabolism, Nobel Prize, Physiology, STEM, Women in Science

The Nobel Prize in Physiology or Medicine 1947

Born: 15 August 1896, Prague, Austria-Hungary (now Czech Republic)

Died: 26 October 1957, St. Louis, MO, USA

Affiliation at the time of the award: Washington University, St. Louis, MO, USA

Prize motivation: "for their discovery of the course of the catalytic conversion of glycogen"

Field: biochemistry, metabolism, physiology

Prize share: jointly to Carl Ferdinand Cori and Gerty Theresa Cori, née Radnitz "for their discovery of the course of the catalytic conversion of glycogen" and the other half to Bernardo Alberto Houssay "for his discovery of the part played by the hormone of the anterior pituitary lobe in the metabolism of sugar".

Note: Dr. Cori's biography was an interesting read. Considering it was penned by the Nobel committee at the end of the 1940's; women were just a few years beyond the Suffrage Movement, and society was still - in general - not nearly as advanced socially or sociologically on cultural or gender issues. I found and give reference to a biography more about her than... well, you'll see what I mean in a moment.

Carl Ferdinand Cori was born in Prague on the Marine Biological Station in Trieste, and it was here that the young Carl spend his childhood. He received an early introduction to science from his father and this was stimulated on summer visits to the Tyrol, to the home of his grandfather, Ferdinand Lippich, Professor of Theoretical Physics at Prague. He studied at the German University of Prague to study medicine. During World War I, he served as a lieutenant in the Sanitary Corps of the Austrian Army on the Italian front; he returned to University, where he studied with his future wife, Gerty, to graduate Doctor Vienna and a year as assistant in pharmacology at the position as biochemist at the State Institute for the Study of appointed Professor of Pharmacology at the Washington University Medical School in St. Louis, where he later became Professor in Biochemistry.

The Cori's have collaborated in most of their research work, commencing in their student days and stemming from their mutual interest in the preclinical sciences. Their first joint paper resulted from an immunological study of the complement of human serum.

"Gerty Cori - Facts". Nobelprize.org. Nobel Media AB 2014. Web. 28 Mar 2015. http://www.nobelprize.org/nobel_prizes/medicine/laureates/1947/cori-gt-facts.html

Changing The Face of Medicine: Dr. Gerty Theresa Radnitz Cori, first woman in America to receive a Nobel Prize in Science