|
Albert J. R. Heck
Albert J.R. Heck (born 25 November 1964) is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He is known for his work on technologies to study proteins in their natural environment, with the aim to understand their biological function. Albert Heck was awarded the Spinoza Prize in 2017, the highest scientific award in the Netherlands. Biography Albert Heck was born in Goes, Netherlands. He studied chemistry at the VU University in Amsterdam, and received his PhD degree from the University of Amsterdam in 1993. After a postdoctoral period at Stanford University in the lab of Richard Zare and Sandia National Laboratories (Livermore) he became a postdoctoral fellow and later lecturer at University of Warwick. In 1998 he accepted a chair at Utrecht University as head of the Biomolecular Mass Spectrometry and Proteomics Group. His group is part of the Departments of Chemistry and Pharmaceutical Sciences of the F ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
University Of Amsterdam
The University of Amsterdam (abbreviated as UvA, nl, Universiteit van Amsterdam) is a public research university located in Amsterdam, Netherlands. The UvA is one of two large, publicly funded research universities in the city, the other being the Vrije Universiteit Amsterdam (VU). Established in 1632 by municipal authorities and later renamed for the city of Amsterdam, the University of Amsterdam is the third-oldest university in the Netherlands. It is one of the largest research universities in Europe with 31,186 students, 4,794 staff, 1,340 PhD students and an annual budget of €600 million. It is the largest university in the Netherlands by enrollment. The main campus is located in central Amsterdam, with a few faculties located in adjacent boroughs. The university is organised into seven faculties: Humanities, Social and Behavioural Sciences, Economics and Business, Science, Law, Medicine, Dentistry. The University of Amsterdam has produced six Nobel Laureates and fiv ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Postdoctoral Fellowship
A postdoctoral fellow, postdoctoral researcher, or simply postdoc, is a person professionally conducting research after the completion of their doctoral studies (typically a PhD). The ultimate goal of a postdoctoral research position is to pursue additional research, training, or teaching in order to have better skills to pursue a career in academia, research, or any other field. Postdocs often, but not always, have a temporary academic appointment, sometimes in preparation for an academic faculty position. They continue their studies or carry out research and further increase expertise in a specialist subject, including integrating a team and acquiring novel skills and research methods. Postdoctoral research is often considered essential while advancing the scholarly mission of the host institution; it is expected to produce relevant publications in peer-reviewed academic journals or conferences. In some countries, postdoctoral research may lead to further formal qualificati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alexander Alexeyevich Makarov
Alexander Alexeyevich Makarov, (born 1966) is a Russian physicist who led the team that developed the Orbitrap, a type of mass spectrometer, and received the 2008 American Society for Mass Spectrometry Distinguished Contribution in Mass Spectrometry Award for this development. In November 2013 he was appointed to Professor by Special Appointment of High Resolution Mass Spectrometry at the Department of Chemistry and the Bijvoet Center for Biomolecular Research of Utrecht University in the Netherlands. As of 2016, he is Director of Global Research for Life Sciences Mass Spectrometry at Thermo Fisher Scientific. Early life and education * 1989 Moscow Engineering Physics Institute - M.S. Molecular Physics * 1993 Moscow Engineering Physics Institute - Ph.D. Physics and Mathematics * 1994-1996 Warwick University - Postdoctoral Appointment Awards * 2008 ASMS Distinguished Contribution in Mass Spectrometry Award * 2012 Thomson Medal Award * 2020 Fellow of the Royal Society F ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NRC Handelsblad
''NRC'', previously called ''NRC Handelsblad'' (), is a daily morning newspaper published in the Netherlands by NRC Media. It is generally accepted as a newspaper of record in the Netherlands. History ''NRC Handelsblad'' was first published on 1 October 1970 after a merger of the Amsterdam newspaper ''Algemeen Handelsblad'' (founded 1828 by J.W. van den Biesen) and the Rotterdam ''Nieuwe Rotterdamsche Courant'' (founded 1844 by Henricus Nijgh). The paper's motto is ''Lux et Libertas'' – Light (referring to the Age of Enlightenment) and Freedom. Editor was succeeded on 12 December 2006, by . After a dispute with the new owners Donker had to step down on 26 April 2010 and was replaced by Belgian . In 2019, he was succeeded by René Moerland. On 7 March 2011, the paper changed its format from broadsheet to tabloid. The circulation of ''NRC Handelsblad'' in 2014 was 188,500 copies, putting it in 4th place among the national dailies. In 2015 the NRC Media group was acquired by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Complement System
The complement system, also known as complement cascade, is a part of the immune system that enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. It is part of the innate immune system, which is not adaptable and does not change during an individual's lifetime. The complement system can, however, be recruited and brought into action by antibodies generated by the adaptive immune system. The complement system consists of a number of small proteins that are synthesized by the liver, and circulate in the blood as inactive precursors. When stimulated by one of several triggers, proteases in the system cleave specific proteins to release cytokines and initiate an amplifying cascade of further cleavages. The end result of this ''complement activation'' or ''complement fixation'' cascade is stimulation of phagocytes to clear foreign and damaged material ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antigen
In immunology, an antigen (Ag) is a molecule or molecular structure or any foreign particulate matter or a pollen grain that can bind to a specific antibody or T-cell receptor. The presence of antigens in the body may trigger an immune response. The term ''antigen'' originally referred to a substance that is an antibody generator. Antigens can be proteins, peptides (amino acid chains), polysaccharides (chains of monosaccharides/simple sugars), lipids, or nucleic acids. Antigens are recognized by antigen receptors, including antibodies and T-cell receptors. Diverse antigen receptors are made by cells of the immune system so that each cell has a specificity for a single antigen. Upon exposure to an antigen, only the lymphocytes that recognize that antigen are activated and expanded, a process known as clonal selection. In most cases, an antibody can only react to and bind one specific antigen; in some instances, however, antibodies may cross-react and bind more than one antigen. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antibodies
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can ''tag'' a microbe or an infected cell for attack by other parts of the immune system, or can neutralize it directly (for example, by blocking a part of a virus that is essential for its invasion). To allow the immune system to recognize millions of different antigens, the antigen-binding sites at both tips of the antibody come in an equally wide variety. In contrast, the remainder of the antibody is relatively constant. It only occurs in a few vari ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribosomes
Ribosomes ( ) are macromolecular machines, found within all cells, that perform biological protein synthesis (mRNA translation). Ribosomes link amino acids together in the order specified by the codons of messenger RNA (mRNA) molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and many ribosomal proteins (RPs or r-proteins). The ribosomes and associated molecules are also known as the ''translational apparatus''. Overview The sequence of DNA that encodes the sequence of the amino acids in a protein is transcribed into a messenger RNA chain. Ribosomes bind to messenger RNAs and use their sequences for determining the correct sequence of amino acids to generate a given protein. Amino acids are selected and carried to the ribosome by transfer RNA (tRNA) molecules, which enter the ribosome and bind to the messenger RNA chain via an anti-cod ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cross-link
In chemistry and biology a cross-link is a bond or a short sequence of bonds that links one polymer chain to another. These links may take the form of covalent bonds or ionic bonds and the polymers can be either synthetic polymers or natural polymers (such as proteins). In polymer chemistry "cross-linking" usually refers to the use of cross-links to promote a change in the polymers' physical properties. When "crosslinking" is used in the biological field, it refers to the use of a probe to link proteins together to check for protein–protein interactions, as well as other creative cross-linking methodologies. Although the term is used to refer to the "linking of polymer chains" for both sciences, the extent of crosslinking and specificities of the crosslinking agents vary greatly. As with all science, there are overlaps, and the following delineations are a starting point to understanding the subtleties. Polymer chemistry Crosslinking is the general term for the process of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Native State
In biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional. The native state of a biomolecule may possess all four levels of biomolecular structure, with the secondary through quaternary structure being formed from weak interactions along the covalently-bonded backbone. This is in contrast to the denatured state, in which these weak interactions are disrupted, leading to the loss of these forms of structure and retaining only the biomolecule's primary structure. Biochemistry Proteins While all protein molecules begin as simple unbranched chains of amino acids, once completed they assume highly specific three-dimensional shapes. That ultimate shape, known as tertiary structure, is the folded shape that possesses a minimum of free energy. It is a protein's tertiary, folded structure that makes it capable of performing its biological function. In fact, shape changes in proteins are the primary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bijvoet Centre For Biomolecular Research
The Bijvoet Centre for Biomolecular Research is a research institute at Utrecht University. The Bijvoet Centre performs research on the relation between the structure and function of biomolecules, including proteins and lipids, which play a role in biological processes such as regulation, interaction and recognition. The Bijvoet Centre houses advanced infrastructures for the analysis of proteins and other biomolecules using NMR, X-ray crystallography, electron microscopy and mass spectrometry. The institute is named after famous Dutch chemist Johannes Martin Bijvoet, who worked at Utrecht University. History Utrecht University and the Netherlands Foundation for Chemical Research (SON, which later became the Chemical Sciences division of NWO, the Netherlands Organisation for Scientific Research) founded the Bijvoet Centre for Biomolecular Research as a joint research institute on March 25, 1988. The goal was to create a centre for research and expertise in structural biology with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
