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Dorothee Kern
Dorothee Kern, (born 1966) is a professor of Biochemistry at Brandeis University and former player for the East German national basketball team. In 2016, she cofounded Relay Therapeutics, a Massachusetts-based drug research company studying the motion of proteins using genomic data and computational biology. In 2020, she cofounded MOMA Therapeutics, a company working on drug discovery. In 2017 she became a member of the German Academy of Sciences Leopoldina, a scientific advisory body to the German government and citizens that serves as a liaison between the German scientific community and the rest of the world. Life and career Early life Born in Halle, a town in former East Germany, to parents Gerhard and Gertraude Hübner, she was an energetic child who began learning to play basketball as early as age seven. She achieved her goal of playing for the East German national basketball team by the time she was a teenager playing the position point guard, and she served as cap ...
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Martin Luther University
Martin Luther University of Halle-Wittenberg (german: Martin-Luther-Universität Halle-Wittenberg), also referred to as MLU, is a public, research-oriented university in the cities of Halle and Wittenberg and the largest and oldest university in the German state of Saxony-Anhalt. MLU offers German and international (English) courses leading to academic degrees such as BA, BSc, MA, MSc, doctoral degrees, and Habilitation. The university was created in 1817 through the merger of the University of Wittenberg (founded in 1502) and the University of Halle (founded in 1694). MLU is named after Protestant reformer Martin Luther, who was a professor in Wittenberg. Today, the university campus is located in Halle, while ''Leucorea Foundation'' in Wittenberg serves as MLU's convention centre. Both Halle and Wittenberg are about one hour from Berlin via the Berlin–Halle railway, which offers Intercity-Express (ICE) trains. History University of Wittenberg (''Universität Wittenbe ...
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United States Ski Team
The U.S. Ski Team, operating under the auspices of U.S. Ski & Snowboard, develops and supports men's and women's athletes in the sports of alpine skiing, freestyle skiing, cross-country, ski jumping, and Nordic combined. Since 1974 the team and association have been headquartered in Park City, Utah. These individuals represent the best athletes in the country for their respective sports and compete as a team at the national, world and Olympic level. History ''*The first U.S. Ski Team was officially named in 1965 for the 1966 season, however the United States participated in skiing at all Olympic Winter Games and sent various athletes to World Championships prior to the '66 season.'' 1860s - 1880s Early Ski Clubs and Ski Tournaments in the U.S. Ski clubs appeared in the United States starting in 1861, in California. Norwegian "snowshoe" downhill races are noted in Sierra and Rocky Mountain mining camps. The Nansen Ski Club of Berlin, New Hampshire, was founded by Norwegian ...
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Biophysical Society
The Biophysical Society is an international scientific society whose purpose is to lead the development and dissemination of knowledge in biophysics. Founded in 1958, the Society currently consists of over 7,500 members in academia, government, and industry. Although the Society is based in the United States, it is an international organization. Overseas members currently comprise over one third of the total. Origins The Biophysical Society was founded in response to the growth of the field of biophysics after World War Two, as well as concerns that the American Physiological Society had become too large to serve the community of biophysicists. Discussions between prominent biophysicists in 1955 and 1956 led to the planning of the society's first meeting in Columbus, Ohio in 1957, with about 500 attendees. Among the scientists involved in the early effort were Ernest C. Pollard, Samuel Talbot, Otto Schmitt, Kenneth Stewart Cole, W. A. Selle, Max Lauffer, Ralph Stacy, Herma ...
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Conformational Change
In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a ''conformational change''. Factors that may induce such changes include temperature, pH, voltage, light in chromophores, concentration of ions, phosphorylation, or the binding of a ligand. Transitions between these states occur on a variety of length scales (tenths of Å to nm) and time scales (ns to s), and have been linked to functionally relevant phenomena such as allosteric signaling and enzyme catalysis. Laboratory analysis Many biophysical techniques such as crystallography, NMR, electron paramagnetic resonance (EPR) using spin label techniques, circular dichroism (CD), hydrogen exchange, and FRET can be used to study macrom ...
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Molecular Machine
A molecular machine, nanite, or nanomachine is a molecular component that produces quasi-mechanical movements (output) in response to specific stimuli (input). In cellular biology, macromolecular machines frequently perform tasks essential for life, such as DNA replication and ATP synthesis. The expression is often more generally applied to molecules that simply mimic functions that occur at the macroscopic level. The term is also common in nanotechnology where a number of highly complex molecular machines have been proposed that are aimed at the goal of constructing a molecular assembler. For the last several decades, chemists and physicists alike have attempted, with varying degrees of success, to miniaturize machines found in the macroscopic world. Molecular machines are at the forefront of cellular biology research. The 2016 Nobel Prize in Chemistry was awarded to Jean-Pierre Sauvage, Sir J. Fraser Stoddart, and Bernard L. Feringa for the design and synthesis of molecular ...
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Academic Tenure
Tenure is a category of academic appointment existing in some countries. A tenured post is an indefinite academic appointment that can be terminated only for cause or under extraordinary circumstances, such as financial exigency or program discontinuation. Tenure is a means of defending the principle of academic freedom, which holds that it is beneficial for society in the long run if scholars are free to hold and examine a variety of views. By country United States and Canada Under the tenure systems adopted by many universities and colleges in the United States and Canada, some faculty positions have tenure and some do not. Typical systems (such as the widely adopted "1940 Statement of Principles on Academic Freedom and Tenure" of the American Association of University Professors) allow only a limited period to establish a record of published research, ability to attract grant funding, academic visibility, teaching excellence, and administrative or community service. They ...
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Biological Computing
Biological computers use biologically derived molecules — such as DNA and/or proteins — to perform digital or real computations. The development of biocomputers has been made possible by the expanding new science of nanobiotechnology. The term nanobiotechnology can be defined in multiple ways; in a more general sense, nanobiotechnology can be defined as any type of technology that uses both nano-scale materials (i.e. materials having characteristic dimensions of 1-100 nanometers) and biologically based materials. A more restrictive definition views nanobiotechnology more specifically as the design and engineering of proteins that can then be assembled into larger, functional structures The implementation of nanobiotechnology, as defined in this narrower sense, provides scientists with the ability to engineer biomolecular systems specifically so that they interact in a fashion that can ultimately result in the computational functionality of a computer. Scientific background B ...
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X-ray Crystallography
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information. Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various mat ...
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Nuclear Magnetic Resonance Spectroscopy
Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. The sample is placed in a magnetic field and the NMR signal is produced by excitation of the nuclei sample with radio waves into nuclear magnetic resonance, which is detected with sensitive radio receivers. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency, thus giving access to details of the electronic structure of a molecule and its individual functional groups. As the fields are unique or highly characteristic to individual compounds, in modern organic chemistry practice, NMR spectroscopy is the definitive method to identify monomolecular organic compounds. The principle of NMR usually involves three sequential steps: # The alignment (polarization) of the magnetic nuclear spins in an applied, constant magnetic field B0. # The ...
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Thiamine
Thiamine, also known as thiamin and vitamin B1, is a vitamin, an essential micronutrient, that cannot be made in the body. It is found in food and commercially synthesized to be a dietary supplement or medication. Phosphorylated forms of thiamine are required for some metabolic reactions, including the breakdown of glucose and amino acids. Food sources of thiamine include whole grains, legumes, and some meats and fish. Grain processing removes much of the vitamin content, so in many countries cereals and flours are enriched with thiamine. Supplements and medications are available to treat and prevent thiamine deficiency and disorders that result from it include beriberi and Wernicke encephalopathy. They are also used to treat maple syrup urine disease and Leigh syndrome. Supplements and medications are typically taken by mouth, but may also be given by intravenous or intramuscular injection. Thiamine supplements are generally well tolerated. Allergic reactions, including ...
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Allosteric Regulation
In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the ''allosteric site'' or ''regulatory site''. Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change and/or a change in protein dynamics. Effectors that enhance the protein's activity are referred to as ''allosteric activators'', whereas those that decrease the protein's activity are called ''allosteric inhibitors''. Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling. Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term ''allostery'' comes from the Ancient Greek ''allos'' (), "other", and ''stereos' ...
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Protein Folding
Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a "folded" conformation by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA to a linear chain of amino acids. At this stage the polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding of many proteins begins even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), ...
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