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Carolyn Cohen
Carolyn Cohen (June 18, 1929 – December 20, 2017) was an American biologist and biophysicist. She was a Fellow of the American Academy of Arts and Sciences. Early life and education Carolyn Cohen was born June 18th, 1929 to parents Anna and Philip Cohen. After Cohen's father died in 1939, she credited his lawyer Samuel Sumner Goldberg for mentoring her and nurturing her curiosity. Cohen attended Joan of Arc Junior High School, then the selective Hunter College High School. After rejections from McGill University and Barnard College, Cohen's French teacher urged her to apply to Bryn Mawr College, where she was accepted with a full-tuition scholarship. In the summer of 1949, Cohen took a job in the kitchen of the Marine Biological Laboratory at Woods Hole, MA. There she met Shinya Inoué, worked for Otto Schmitt, and attended a lecture by Dorothy Wrinch that she later credited with stimulating her career interest in protein structures. Cohen completed her Bachelor of Arts in Biolog ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
American Academy Of Arts And Sciences
The American Academy of Arts and Sciences (abbreviation: AAA&S) is one of the oldest learned societies in the United States. It was founded in 1780 during the American Revolution by John Adams, John Hancock, James Bowdoin, Andrew Oliver, and other Founding Fathers of the United States. It is headquartered in Cambridge, Massachusetts. Membership in the academy is achieved through a thorough petition, review, and election process. The academy's quarterly journal, ''Dædalus'', is published by MIT Press on behalf of the academy. The academy also conducts multidisciplinary public policy research. History The Academy was established by the Massachusetts legislature on May 4, 1780, charted in order "to cultivate every art and science which may tend to advance the interest, honor, dignity, and happiness of a free, independent, and virtuous people." The sixty-two incorporating fellows represented varying interests and high standing in the political, professional, and commercial secto ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Actin
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm. An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division. Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell sign ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Brandeis University
, mottoeng = "Truth even unto its innermost parts" , established = , type = Private research university , accreditation = NECHE , president = Ronald D. Liebowitz , provost = Carol Fierke , city = Waltham , state = Massachusetts , country = United States , endowment = $1.07 billion (2019) , students = 5,458 (2021) , undergrad = 3,591 (2021) , postgrad = 1,967 (2021) , faculty = 544 (2021) , administrative_staff = 1,314 (2021) , campus = Small City, , mascot = The Judge and Ollie the Owl (named for Justice Oliver Wendell Holmes Jr.) , sports_nickname = Judges , colors = Brandeis Blue , athletics_affiliations = , academic_affiliations = , website = , logo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Microscopy
An electron microscope is a microscope that uses a beam of accelerated electrons as a source of illumination. As the wavelength of an electron can be up to 100,000 times shorter than that of visible light photons, electron microscopes have a higher resolving power than light microscopes and can reveal the structure of smaller objects. A scanning transmission electron microscope has achieved better than 50 pm resolution in annular dark-field imaging mode and magnifications of up to about 10,000,000× whereas most light microscopes are limited by diffraction to about 200 nm resolution and useful magnifications below 2000×. Electron microscopes use shaped magnetic fields to form electron optical lens systems that are analogous to the glass lenses of an optical light microscope. Electron microscopes are used to investigate the ultrastructure of a wide range of biological and inorganic specimens including microorganisms, cells, large molecules, biopsy samples, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Henry S
Henry may refer to: People *Henry (given name) *Henry (surname) * Henry Lau, Canadian singer and musician who performs under the mononym Henry Royalty * Portuguese royalty ** King-Cardinal Henry, King of Portugal ** Henry, Count of Portugal, Henry of Burgundy, Count of Portugal (father of Portugal's first king) ** Prince Henry the Navigator, Infante of Portugal ** Infante Henrique, Duke of Coimbra (born 1949), the sixth in line to Portuguese throne * King of Germany **Henry the Fowler (876–936), first king of Germany * King of Scots (in name, at least) ** Henry Stuart, Lord Darnley (1545/6–1567), consort of Mary, queen of Scots ** Henry Benedict Stuart, the 'Cardinal Duke of York', brother of Bonnie Prince Charlie, who was hailed by Jacobites as Henry IX * Four kings of Castile: **Henry I of Castile **Henry II of Castile **Henry III of Castile **Henry IV of Castile * Five kings of France, spelt ''Henri'' in Modern French since the Renaissance to italianize the name and to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coiled Coil
A coiled coil is a structural motif in proteins in which 2–7 alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) Many coiled coil-type proteins are involved in important biological functions, such as the regulation of gene expression — e.g., transcription factors. Notable examples are the oncoproteins c-Fos and c-Jun, as well as the muscle protein tropomyosin. Discovery The possibility of coiled coils for α-keratin was initially somewhat controversial. Linus Pauling and Francis Crick independently came to the conclusion that this was possible at about the same time. In the summer of 1952, Pauling visited the laboratory in England where Crick worked. Pauling and Crick met and spoke about various topics; at one point, Crick asked whether Pauling had considered "coiled coils" (Crick came up with the term), to which Pauling said he had. Upon returning to the United States, Pauling resumed research on the topic. He conc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kenneth Holmes
Kenneth Charles Holmes FRS (1934 – 2 November 2021) was a British molecular biologist. He was born in Hammersmith, London. He was a former colleague of Rosalind Franklin at Birkbeck College with Aaron Klug and John Finch and moved to the Laboratory of Molecular Biology, Cambridge in 1962. From 1975 and 1976 he was acting Head of Outstation, EMBL Synchrotron Radiation Laboratory at DESY, Hamburg. He worked at the Max Planck Institute for Medical Research as an "Emeritus Scientific Member". In 1981, he was elected a Fellow of the Royal Society, and was awarded their 1997 Gabor Medal which is of silver gilt and then accompanied by 1,000 pounds "in recognition of his achievements in molecular biology, in particular his pioneering analyses of biological structures and viruses, and his development of the use of synchrotron radiation for X-ray diffraction experiments, now a widely used technique not only in molecular biology but in physics and materials science". He was awarded ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mytilus Edulis
The blue mussel (''Mytilus edulis''), also known as the common mussel, is a medium-sized edible marine (ocean), marine bivalve mollusc in the family (biology), family Mytilidae, the mussels. Blue mussels are subject to commercial use and intensive aquaculture. A species with a large range, empty shells are commonly found on beaches around the world. Systematics and distribution The ''Mytilus edulis'' complex Systematically blue mussel consists of a group of (at least) three closely related taxa of mussels, known as the ''Mytilus edulis'' complex. Collectively they occupy both coasts of the North Atlantic (including the Mediterranean) and of the North Pacific in temperate to polar waters, as well as coasts of similar nature in the Southern Hemisphere. The distribution of the component taxa has been recently modified as a result of human activity. The taxa can hybridise with each other, if present at the same locality. *''Mytilus edulis'' sensu stricto: Native to the North Atla ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astbur ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Susan Lowey
Susan Lowey (born 22 January 1933 in Vienna) is an American biophysicist researching the structure and function of contractile proteins. She currently teaches in the Department of Molecular Physiology & Biophysics at the University of Vermont and is a fellow of the American Academy of Arts and Sciences as well as the Biophysical Society. Education Lowey received her BA from Barnard College, PhD in Physical Chemistry from Yale University and pursued post-doctoral research at Harvard University on the biochemistry and structure of myosin, a protein involved in muscle contraction. Career Lowey was employed for about a decade at the Children's Cancer Research Foundation and Harvard Medical School. In 1972, Lowey became a faculty member at The Rosenstiel Basic Medical Sciences Research Center, Brandeis University to collaborate with biophysicists. In 1998, Lowey was appointed as a faculty member in the Department of Molecular Physiology & Biophysics at the University of Vermont. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dana–Farber Cancer Institute
Dana–Farber Cancer Institute is a comprehensive cancer treatment and research institution in Boston, Massachusetts. Dana–Farber is the founding member of Dana–Farber/Harvard Cancer Center, Harvard's Comprehensive Cancer Center designated by the National Cancer Institute, and one of the 15 clinical affiliates and research institutes of Harvard Medical School. As of 2021, Dana–Farber is ranked the #3 cancer hospital in the world. Two Nobel laureates in Physiology or Medicine are among its past and present faculty. Dana–Farber's research discoveries include the development of the highly successful Gleevec to treat chronic myeloid leukemia. Overview Dana–Farber employs more than 4,855 full-time and part-time people, 529 faculty, and has annual gross revenues of about $1,733,386,000. All faculty and postdoctoral research fellows at Dana–Farber hold the equivalent academic positions concurrently at Harvard University. There are more than 523,425 adult and pediatric patie ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tropomyosin
Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in actin-based cytoskeletons. Tropomyosin and the actin skeleton All organisms contain organelles that provide physical integrity to their cells. These type of organelles are collectively known as the cytoskeleton, and one of the most ancient systems is based on filamentous polymers of the protein actin. A polymer of a second protein, tropomyosin, is an integral part of most actin filaments in animals. Tropomyosins are a large family of integral components of actin filaments that play a critical role in regulating the function of actin filaments in both muscle and nonmuscle cells. These proteins consist of rod-shaped coiled-coil hetero- or homo- dimers that lie along the α-helical groove of most actin filaments. Interaction occurs along the length of the actin filament, with dimers aligning in a head-to-tail fashion. Tropomyosins are often categorised into two groups, muscle tropomyosin isoforms and nonmus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
