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Structural Biology
Structural biology is a field that is many centuries old which, and as defined by the Journal of 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 microscopy. Through the discovery of 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, NMR spectroscopy allowed information about p ...
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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 variou ...
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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); or ...
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Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many texts consider myoglobin not to be found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray cryst ...
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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 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.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. 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 polypep ...
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Theodor Svedberg
Theodor Svedberg (30 August 1884 – 25 February 1971) 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 education, Svedberg entered a ch ...
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James Watson
James Dewey Watson (born April 6, 1928) is an American molecular biologist, geneticist, and zoologist. In 1953, he co-authored with Francis Crick the academic paper proposing the 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". In subsequent years, it has been recognized that Watson and his colleagues did not properly attribute colleague Rosalind Franklin for her contributions to the discovery of the double helix structure. Watson earned degrees at the University of Chicago ( BS, 1947) and Indiana University (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 ...
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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 helical structure of the DNA molecule. Crick and Watson's paper in ''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 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 proteins, it cannot flow back to nucleic acids. In other wor ...
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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, and to the development of radar. He is best known for his work at King's College London on the structure of DNA. Wilkins' work on DNA falls into two distinct phases. The first was in 1948–1950, when his initial studies produced the first clear X-ray images of DNA, which he presented at a conference in Naples in 1951 attended by James Watson. During the second phase, 1951–52, Wilkins produced clear "B form" "X" shaped images from squid sperm, images he sent to James Watson and Francis Crick, causing Watson to write "Wilkins... has obtained extremely excellent X-ray diffraction photographs" f DNA In 1953, Wilkins' group coordinator Sir John Randall ...
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Rosalind Franklin
Rosalind Elsie Franklin (25 July 192016 April 1958) was a British chemist and X-ray crystallographer whose 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, her contributions to the discovery of the structure of DNA were largely unrecognized during her life, for which she 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". She graduated in 1941 with a degree in 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 under the British Coal Utilisation Research ...
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Diffraction
Diffraction is defined as the interference or bending of waves around the corners of an obstacle or through an aperture into the region of geometrical shadow of the obstacle/aperture. The diffracting object or aperture effectively becomes a secondary source of the propagating wave. Italian scientist Francesco Maria Grimaldi coined the word ''diffraction'' and was the first to record accurate observations of the phenomenon in 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 bending pattern is most pronounced when a wave from a coherent source (such as a laser) encounters a slit/aperture that is comparable in size to its wavelength, as shown in the inserted image. This is due to the addition, or interference, of different points on the wavefront (or, equivalently, each wavelet) that travel by paths of di ...
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Copper Sulfate
Copper sulfate may refer to: * Copper(II) sulfate, CuSO4, a common compound used as a fungicide and herbicide * Copper(I) sulfate Copper(I) sulfate, also known as cuprous sulfate, is an inorganic compound with the chemical formula Cu2 SO4. It is a white solid that has attracted little attention, in contrast to copper(II) sulfate. It is an unusual example of a copper(I) ..., Cu2SO4, which is uncommonly used * Copper(II) sulfate, CuSO4 is greenish blue Copper compounds {{Chem-stub ...
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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 diffraction of X-rays by crystals. In addition to his scientific endeavors with contributions in optics, crystallography, quantum theory, superconductivity, and the theory of relativity, Laue had a number of administrative positions which advanced and guided 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 Strassburg, he began his compulsory year of military service, after which in 1899 he started to study mathematics, physics, and chemistry at the University of Strassburg, the University of Göttingen, and the Ludwig Maximilian ...
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