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Structural Biology
Structural biology deals with structural analysis of living material (formed, composed of, and/or maintained and refined by living cells) at every level of organization. Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes. In the 20th century, a variety of experimental techniques were developed to examine the 3D structures of biological molecules. The most prominent techniques are X-ray crystallography, nuclear magnetic resonance, and Electron microscope, electron microscopy. Through the discovery of X-ray, X-rays and its applications to protein crystals, structural biology was revolutionized, as now scientists could obtain the three-dimensional structures of biological molecules in atomic detail. Likewise, Nuclear magnetic resonance spectroscopy, NMR spectroscopy allowed information about protein structure and dynamic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
X-ray Crystallography
X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to Diffraction, diffract in specific directions. By measuring the angles and intensities of the X-ray diffraction, a crystallography, crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and the positions of the atoms, as well as their chemical bonds, crystallographic disorder, and other information. 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 between various materials, especially minerals and alloys. The method has also revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystall ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molecular Model
A molecular model is a physical model of an atomistic system that represents molecules and their processes. They play an important role in understanding chemistry and generating and testing hypotheses. The creation of mathematical models of molecular properties and behavior is referred to as molecular modeling, and their graphical depiction is referred to as molecular graphics. The term, "molecular model" refer to systems that contain one or more explicit atoms (although solvent atoms may be represented implicitly) and where nuclear structure is neglected. The electronic structure is often also omitted unless it is necessary in illustrating the function of the molecule being modeled. Molecular models may be created for several reasons – as pedagogic tools for students or those unfamiliar with atomistic structures; as objects to generate or test theories (e.g., the structure of DNA); as analogue computers (e.g., for measuring distances and angles in flexible systems); o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Tertiary Structure
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demonstr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Theodor Svedberg
Theodor Svedberg (30 August 1884 – 25 February 1971; also known as The Svedberg) was a Swedish chemist and Nobel laureate for his research on colloids and proteins using the ultracentrifuge. Svedberg was active at Uppsala University from the mid-1900s to late 1940s. While at Uppsala, Svedberg started as a docent before becoming the university's physical chemistry head in 1912. After leaving Uppsala in 1949, Svedberg was in charge of the Gustaf Werner Institute until 1967. Apart from his 1926 Nobel Prize, Svedberg was named a Foreign Member of the Royal Society in 1944 and became part of the National Academy of Sciences in 1945. Early life and education Svedberg was born in Valbo, Sweden on 30 August 1884. He was the son of Augusta Alstermark and Elias Svedberg. Growing up, Svedberg enjoyed botany and other branches of science. While in grammar school, Svedberg conducted individual laboratorial research and performed scientific demonstrations. For his post-secondary educati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pepsin
Pepsin is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. It is one of three principal endopeptidases (enzymes cutting proteins in the middle) in the human digestive system, the other two being chymotrypsin and trypsin. There are also exopeptidases which remove individual amino acids at both ends of proteins (carboxypeptidases produced by the pancreas and aminopeptidases secreted by the small intestine). During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. The cleavage specificity o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
James Watson
James Dewey Watson (born April 6, 1928) is an American molecular biology, molecular biologist, geneticist, and zoologist. In 1953, he co-authored with Francis Crick the academic paper in ''Nature (journal), Nature'' proposing the Nucleic acid double helix, double helix structure of the DNA molecule. Watson, Crick and Maurice Wilkins were awarded the 1962 Nobel Prize in Physiology or Medicine "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material". Watson earned degrees at the University of Chicago (Bachelor of Science, 1947) and Indiana University Bloomington (PhD, 1950). Following a post-doctoral year at the University of Copenhagen with Herman Kalckar and Ole Maaløe, Watson worked at the University of Cambridge's Cavendish Laboratory in England, where he first met his future collaborator Francis Crick. From 1956 to 1976, Watson was on the faculty of the Harvard University Biology Department ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Francis Crick
Francis Harry Compton Crick (8 June 1916 – 28 July 2004) was an English molecular biologist, biophysicist, and neuroscientist. He, James Watson, Rosalind Franklin, and Maurice Wilkins played crucial roles in deciphering the Nucleic acid double helix, helical structure of the DNA molecule. Crick and Watson's paper in ''Nature (journal), Nature'' in 1953 laid the groundwork for understanding DNA structure and functions. Together with Maurice Wilkins, they were jointly awarded the 1962 Nobel Prize in Physiology or Medicine "for their discoveries concerning the molecular geometry, molecular structure of nucleic acids and its significance for information transfer in living material". Crick was an important theoretical molecular biologist and played a crucial role in research related to revealing the helical structure of DNA. He is widely known for the use of the term "central dogma" to summarise the idea that once information is transferred from nucleic acids (DNA or RNA) to prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Maurice Wilkins
Maurice Hugh Frederick Wilkins (15 December 1916 – 5 October 2004) was a New Zealand-born British biophysicist and Nobel laureate whose research spanned multiple areas of physics and biophysics, contributing to the scientific understanding of phosphorescence, isotope separation, optical microscopy, and X-ray diffraction. He is most noted for initiating and leading early X-ray diffraction studies on DNA at King's College London, and for his pivotal role in enabling the discovery of the double helix structure of DNA. Wilkins began investigating nucleic acids in 1948. By 1950, he and his team had produced some of the first high-quality X-ray diffraction images of DNA fibers. He presented this work in 1951 at a conference in Naples, where it significantly influenced James Watson, prompting Watson to pursue DNA structure research with Francis Crick. In 1951, Rosalind Franklin joined King’s College and was assigned to the same DNA project, though without a clear delineation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rosalind Franklin
Rosalind Elsie Franklin (25 July 192016 April 1958) was a British chemist and X-ray crystallographer. Her work was central to the understanding of the molecular structures of DNA (deoxyribonucleic acid), RNA (ribonucleic acid), viruses, coal, and graphite. Although her works on coal and viruses were appreciated in her lifetime, Franklin's contributions to the discovery of the structure of DNA were largely unrecognised during her life, for which Franklin has been variously referred to as the "wronged heroine", the "dark lady of DNA", the "forgotten heroine", a "feminist icon", and the "Sylvia Plath of molecular biology". Franklin graduated in 1941 with a degree in Natural Sciences (Cambridge), natural sciences from Newnham College, Cambridge, and then enrolled for a PhD in physical chemistry under Ronald George Wreyford Norrish, the 1920 Chair of Physical Chemistry at the University of Cambridge. Disappointed by Norrish's lack of enthusiasm, she took up a research position und ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diffraction
Diffraction is the deviation of waves from straight-line propagation without any change in their energy due to an obstacle or through an aperture. The diffracting object or aperture effectively becomes a secondary source of the Wave propagation, propagating wave. Diffraction is the same physical effect as Wave interference, interference, but interference is typically applied to superposition of a few waves and the term diffraction is used when many waves are superposed. Italian scientist Francesco Maria Grimaldi coined the word ''diffraction'' and was the first to record accurate observations of the phenomenon in 1660 in science, 1660. In classical physics, the diffraction phenomenon is described by the Huygens–Fresnel principle that treats each point in a propagating wavefront as a collection of individual spherical wavelets. The characteristic pattern is most pronounced when a wave from a Coherence (physics), coherent source (such as a laser) encounters a slit/aperture tha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Copper Sulfate
Copper sulfate may refer to: * Copper(II) sulfate, CuSO4, a common, greenish blue compound used as a fungicide and herbicide * Copper(I) sulfate, Cu2SO4, an unstable white solid which is uncommonly used {{chemistry index Copper compounds ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Max Von Laue
Max Theodor Felix von Laue (; 9 October 1879 – 24 April 1960) was a German physicist who received the Nobel Prize in Physics in 1914 "for his discovery of the X-ray diffraction, diffraction of X-rays by crystals". In addition to his scientific endeavors with contributions in optics, crystallography, Quantum mechanics, quantum theory, superconductivity, and the theory of relativity, Laue had a number of administrative positions which advanced and guided Science and technology in Germany, German scientific research and development during four decades. A strong objector to Nazism, he was instrumental in re-establishing and organizing German science after World War II. Biography Early years Laue was born in Pfaffendorf, now part of Koblenz, Germany, to Julius Laue and Minna Zerrenner. In 1898, after passing his ''Abitur'' in Strasbourg, Strassburg, he began his compulsory year of military service, after which in 1899 he started to study mathematics, physics, and chemistry at the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
