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Phage Display
Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein– DNA interactions that uses bacteriophages (viruses that infect bacteria) to connect proteins with the genetic information that encodes them. In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on its outside while containing the gene for the protein on its inside, resulting in a connection between genotype and phenotype. These displaying phages can then be screened against other proteins, peptides or DNA sequences, in order to detect interaction between the displayed protein and those other molecules. In this way, large libraries of proteins can be screened and amplified in a process called ''in vitro'' selection, which is analogous to natural selection. The most common bacteriophages used in phage display are M13 and fd filamentous phage, though T4, T7, and λ phage have ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phage Display
Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein– DNA interactions that uses bacteriophages (viruses that infect bacteria) to connect proteins with the genetic information that encodes them. In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on its outside while containing the gene for the protein on its inside, resulting in a connection between genotype and phenotype. These displaying phages can then be screened against other proteins, peptides or DNA sequences, in order to detect interaction between the displayed protein and those other molecules. In this way, large libraries of proteins can be screened and amplified in a process called ''in vitro'' selection, which is analogous to natural selection. The most common bacteriophages used in phage display are M13 and fd filamentous phage, though T4, T7, and λ phage have ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Filamentous Bacteriophage Fd
The word filament, which is descended from Latin ''filum'' meaning " thread", is used in English for a variety of thread-like structures, including: Astronomy * Galaxy filament, the largest known cosmic structures in the universe * Solar filament, a solar prominence seen against the disc of the sun Biology * Myofilament, filaments of myofibrils constructed from proteins * Protein filament, a long chain of protein subunits, such as those found in hair or muscle * Part of a stamen, the male part of a flower * Hypha, a thread-like cell in fungi and Actinobacteria * Filamentation, an elongation of individual bacterial cells Textiles * Fiber, natural or manmade substances significantly longer than they are wide * Yarn (more loosely) * Filament fiber, fiber that comes in a continuous long length Media * ''Filament'' (magazine), a female-oriented erotica magazine * 2002 movie by Jinsei Tsuji * Filament (band), a musical group from Japan * Filament Games, a Wisconsin-based educat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
German Cancer Research Center
The German Cancer Research Center (known as the Deutsches Krebsforschungszentrum or simply DKFZ in German) is a national cancer research center based in Heidelberg, Germany. It is a member of the Helmholtz Association of German Research Centres, the largest scientific organization in Germany. History The establishment of a national cancer research center in Germany was initiated by Heidelberg surgeon . The DKFZ was set up in 1964 by resolution of the State government of Baden-Württemberg as a foundation under public law. In 1975, the Center became a member of the Association of National Research Centers ("Arbeitsgemeinschaft der Großforschungseinrichtungen") which was transformed into the Hermann von Helmholtz Association of National Research Centers in 1995. The Center has also been a member of the Deutsche Forschungsgemeinschaft (DFG) since 1977. Two scientists to date that were affiliated with the DKFZ have received Nobel Prizes. The first was Harald zur Hausen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scripps Research Institute
Scripps Research, previously known as The Scripps Research Institute (TSRI), is a nonprofit American medical research facility that focuses on research and education in the biomedical sciences. Headquartered in San Diego, California, the institute has over 170 laboratories employing 2,100 scientists, technicians, graduate students, and administrative and other staff, making it the largest private, non-profit biomedical research organization in the United States and among the largest in the world. The institute holds over 1,100 patents, has produced 11 FDA-approved therapeutics, and has generated over 50 spin-off companies. According to the 2017 Nature Innovation Index, Scripps Research is the #1 most influential research institution in the world. The Scripps Research graduate program is ranked 9th nationally in the biological sciences, 6th for organic chemistry, and 6th for biochemistry. In 2022, their Jupiter, FL campus became a part of the University of Florida. Jupiter-base ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
John McCafferty
John McCafferty is a British scientist, one of the founders of Cambridge Antibody Technology alongside Sir Gregory Winter and David Chiswell. He is well known as one of the inventors of scFv antibody fragment phage display, a technology that revolutionised the monoclonal antibody drug discovery. McCafferty and his team developed this process following failures previously generating antibodies by immunizing mice. Later improvements of antibody phage display technology enables the display of millions of different antibody fragments on the surface of filamentous phage (better known as antibody phage library) and subsequent selection of highly specific recombinant antibodies to any given target. This technology is widely exploited in pharmaceutical industry for the discovery and development of therapeutic monoclonal antibodies to treat mainly cancer, inflammatory and infectious diseases. One of the most successful was HUMIRA (adalimumab), discovered by Cambridge Antibody Technology as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Greg Winter
Sir Gregory Paul Winter (born 14 April 1951) is a Nobel Prize-winning English molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England. He is credited with having invented techniques to both humanise (1986) and, later, to fully humanise using phage display, antibodies for therapeutic uses.ThScientific Founders of Bicycle Therapeutics Ltd. – Christian Heinis and Sir Greg Winter, FRS. Previously, antibodies had been derived from mice, which made them difficult to use in human therapeutics because the human immune system had anti-mouse reactions to them. For these developments Winter was awarded the 2018 Nobel Prize in Chemistry along with George Smith and Frances Arnold. He is a Fellow of Trinity College, Cambridge and was appointed Master of Trinity College, Cambridge on 2 Octobe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Laboratory Of Molecular Biology
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health. A new replacement building constructed close by to the original site on the Cambridge Biomedical Campus was opened by Her Majesty the Queen in May 2013. The road outside the new building is named Francis Crick Avenue after the 1962 joint Nobel Prize winner and LMB alumnus, who co-discovered the helical structure of DNA in 1953. History Origins: 1947-61 Max Perutz, following undergraduate training in organic chemistry, left Austria in 1936 and came to the Univer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biopanning
Biopanning is an affinity selection technique which selects for peptides that bind to a given target. All peptide sequences obtained from biopanning using combinatorial peptide libraries have been stored in a special freely available database nameBDB This technique is often used for the selection of antibodies too. Biopanning involves 4 major steps for peptide selection. The first step is to have phage display libraries prepared. This involves inserting foreign desired gene segments into a region of the bacteriophage genome, so that the peptide product will be displayed on the surface of the bacteriophage virion. The most often used are genes pIII or pVIII of bacteriophage M13.Smith GP, and Scott JK. ''Libraries of peptides and proteins displayed on filamentous phage''. Methods in Enzymology. 1993. 217:228-257 The next step is the capturing step. It involves conjugating the phage library to the desired target. This procedure is termed panning. It utilizes the binding interactions ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Capsid
A capsid is the protein shell of a virus, enclosing its genetic material. It consists of several oligomeric (repeating) structural subunits made of protein called protomers. The observable 3-dimensional morphological subunits, which may or may not correspond to individual proteins, are called capsomeres. The proteins making up the capsid are called capsid proteins or viral coat proteins (VCP). The capsid and inner genome is called the nucleocapsid. Capsids are broadly classified according to their structure. The majority of the viruses have capsids with either helical or icosahedral structure. Some viruses, such as bacteriophages, have developed more complicated structures due to constraints of elasticity and electrostatics. The icosahedral shape, which has 20 equilateral triangular faces, approximates a sphere, while the helical shape resembles the shape of a spring, taking the space of a cylinder but not being a cylinder itself. The capsid faces may consist of one or m ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fusion Protein
Fusion proteins or chimeric (kī-ˈmir-ik) proteins (literally, made of parts from different sources) are proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this '' fusion gene'' results in a single or multiple polypeptides with functional properties derived from each of the original proteins. ''Recombinant fusion proteins'' are created artificially by recombinant DNA technology for use in biological research or therapeutics. '' Chimeric'' or ''chimera'' usually designate hybrid proteins made of polypeptides having different functions or physico-chemical patterns. ''Chimeric mutant proteins'' occur naturally when a complex mutation, such as a chromosomal translocation, tandem duplication, or retrotransposition creates a novel coding sequence containing parts of the coding sequences from two different genes. Naturally occurring fusion proteins are commonly found in cancer cells, where they may function as oncopro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
George Smith (chemist)
George Pearson Smith (born 10 March 1941) is an American biologist and Nobel laureate. He is a Curators' Distinguished Professor Emeritus of Biological Sciences at the University of Missouri in Columbia, Missouri, US. Career Born in Norwalk, Connecticut, he earned his A.B. degree from Haverford College in biology, was a high school teacher and lab technician for a year, and earned his PhD degree in bacteriology and immunology from Harvard University. He was a postdoc at the University of Wisconsin (with future Nobel laureate Oliver Smithies) before moving to Columbia, Missouri and joining the University of Missouri faculty in 1975. He spent the 1983–1984 academic year at Duke University with Robert Webster where he began the work that led to him being awarded a Nobel Prize. He is best known for phage display, a technique where a specific protein sequence is artificially inserted into the coat protein gene of a bacteriophage, causing the protein to be expressed on the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lambda Phage
''Enterobacteria phage λ'' (lambda phage, coliphage λ, officially ''Escherichia virus Lambda'') is a bacterial virus, or bacteriophage, that infects the bacterial species ''Escherichia coli'' (''E. coli''). It was discovered by Esther Lederberg in 1950. The wild type of this virus has a temperate life cycle that allows it to either reside within the genome of its host through lysogeny or enter into a lytic phase, during which it kills and lyses the cell to produce offspring. Lambda strains, mutated at specific sites, are unable to lysogenize cells; instead, they grow and enter the lytic cycle after superinfecting an already lysogenized cell. The phage particle consists of a head (also known as a capsid), a tail, and tail fibers (see image of virus below). The head contains the phage's double-strand linear DNA genome. During infection, the phage particle recognizes and binds to its host, ''E. coli'', causing DNA in the head of the phage to be ejected through the tail into t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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