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Affinity Capture
Affinity capture is a technique in molecular biology used to isolate desired compounds based on their chemical properties and a solid substrate. Commonly, plates out of solid materials such as glass are coated with various reagents to allow for covalent bonding of a capturing molecule such as an antibody. Afterwards, a solvent containing a desired compound for isolation is poured onto the plate, and the compound binds to the receptors on the plate (hence the capturing of the compound). Washing the plate and removing the desired compound completes the purification process. Applications Affinity capture has been used to isolate proteins by means of binding a peptide sequence to the solid substrate, thus allowing for protein capture. The process has also been examined for potential automation, but the unique circumstances for any given experiment may impede reproducibility Reproducibility, closely related to replicability and repeatability, is a major principle underpinning the scien ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molecular Biology
Molecular biology is a branch of biology that seeks to understand the molecule, molecular basis of biological activity in and between Cell (biology), cells, including biomolecule, biomolecular synthesis, modification, mechanisms, and interactions. Though cells and other microscopic structures had been observed in living organisms as early as the 18th century, a detailed understanding of the mechanisms and interactions governing their behavior did not emerge until the 20th century, when technologies used in physics and chemistry had advanced sufficiently to permit their application in the biological sciences. The term 'molecular biology' was first used in 1945 by the English physicist William Astbury, who described it as an approach focused on discerning the underpinnings of biological phenomena—i.e. uncovering the physical and chemical structures and properties of biological molecules, as well as their interactions with other molecules and how these interactions explain observ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chemical Affinity
In chemical physics and physical chemistry, chemical affinity is the electronic property by which dissimilar chemical species are capable of forming chemical compounds. Chemical affinity can also refer to the tendency of an atom or compound to combine by chemical reaction with atoms or compounds of unlike composition. History Early theories The idea of ''affinity'' is extremely old. Many attempts have been made at identifying its origins. The majority of such attempts, however, except in a general manner, end in futility since "affinities" lie at the basis of all Magic (paranormal), magic, thereby pre-dating science. Physical chemistry, however, was one of the first branches of science to study and formulate a "theory of affinity". The name ''affinitas'' was first used in the sense of chemical relation by German philosopher Albertus Magnus near the year 1250. Later, those as Robert Boyle, John Mayow, Johann Glauber, Isaac Newton, and Georg Stahl put forward ideas on elective ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Covalent Bonding
A covalent bond is a chemical bond that involves the sharing of electrons to form electron pairs between atoms. These electron pairs are known as shared pairs or bonding pairs. The stable balance of attractive and repulsive forces between atoms, when they share electrons, is known as covalent bonding. For many molecules, the sharing of electrons allows each atom to attain the equivalent of a full valence shell, corresponding to a stable electronic configuration. In organic chemistry, covalent bonding is much more common than ionic bonding. Covalent bonding also includes many kinds of interactions, including σ-bonding, π-bonding, metal-to-metal bonding, agostic interactions, bent bonds, three-center two-electron bonds and three-center four-electron bonds. The term "covalence" was introduced by Irving Langmuir in 1919, with Nevil Sidgwick using "co-valent link" in the 1920s. Merriam-Webster dates the specific phrase ''covalent bond'' to 1939, recognizing its first known u ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antibody
An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as pathogenic bacteria, bacteria and viruses, including those that cause disease. Each individual antibody recognizes one or more specific antigens, and antigens of virtually any size and chemical composition can be recognized. Antigen literally means "antibody generator", as it is the presence of an antigen that drives the formation of an antigen-specific antibody. Each of the branching chains comprising the "Y" of an antibody contains a paratope that specifically binds to one particular epitope on an antigen, allowing the two molecules to bind together with precision. Using this mechanism, antibodies can effectively "tag" the antigen (or a microbe or an infected cell bearing such an antigen) for attack by cells of the immune system, or can neutralize it directly (for example, by blocking a p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reproducibility
Reproducibility, closely related to replicability and repeatability, is a major principle underpinning the scientific method. For the findings of a study to be reproducible means that results obtained by an experiment or an observational study or in a statistical analysis of a data set should be achieved again with a high degree of reliability when the study is replicated. There are different kinds of replication but typically replication studies involve different researchers using the same methodology. Only after one or several such successful replications should a result be recognized as scientific knowledge. History The first to stress the importance of reproducibility in science was the Anglo-Irish chemist Robert Boyle, in England in the 17th century. Boyle's air pump was designed to generate and study vacuum, which at the time was a very controversial concept. Indeed, distinguished philosophers such as René Descartes and Thomas Hobbes denied the very possibility of vacuum ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chem-seq
Chem-seq is a technique that is used to map genome-wide interactions between small molecules and their protein targets in the chromatin of eukaryotic cell nuclei. The method employs chemical affinity capture coupled with massively parallel DNA sequencing to identify genomic sites where small molecules interact with their target proteins or DNA. It was first described by Lars Anders et al. in the January, 2014 issue of "Nature Biotechnology". Uses of Chem-seq A substantial number of small-molecule ligands, including therapeutic drugs, elicit their effects by binding specific proteins associated with the genome. Mapping the global interactions of these chemical entities with chromatin in a genome-wide manner could provide insights into the mechanisms by which a small molecule influences cellular functions. When combined with other chromatin analysis techniques such as ChIP-seq, Chem-seq can be utilized to investigate the genome-wide effects of therapeutic modalities and to understa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
