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Flow-induced Dispersion Analysis
Flow-induced dispersion analysis (FIDA) is an immobilization-free technology used for characterization and quantification of biomolecular interaction and protein concentration under native conditions. In the FIDA assay, the size of a ligand (indicator) with affinity to the target analyte is measured. When the indicator interacts with the analyte the apparent size increases and this change in size can be used to determine the analyte concentration and interaction. Additionally, the hydrodynamic radius of the analyte-indicator complex is obtained. A FIDA assay is typically completed in minutes and only requires a modest sample consumption of a few μL. Applications * Quantification of analytes (e.g. proteins, peptides, DNA, nanoparticles) in complex solutions (e.g. plasma and fermentation broth ) * Determination of ** affinity constants ** binding kinetics ** molecular size (hydrodynamic radius) **oligomeric state ** diffusion coefficient Principle The FIDA principle is based ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FIDA Principle
''Fida'' (translation: ''Infatuated'') is a 2004 Indian Hindi-language romantic action thriller film directed by Ken Ghosh, starring Fardeen Khan, Kareena Kapoor, Shahid Kapoor and Akhilendra Mishra. The film was released on 20 August 2004. Plot The film starts with someone emptying the bank accounts of many people, including Babu Anna, an underworld don, via an Internet theft. The police are clueless about the robber, and Anna wants revenge. Desperately wanting his money back, Anna assigns his men to find that hacker. The film then shifts to a young man named Jai Malhotra who lives with his best friend, Sonia. One day he sees a woman named Neha Mehra and falls madly in love with her instantly. At first, Neha rejects Jai's advances and this causes him to attempt suicide and prior to that he carves "I love you Neha" on his hand with a knife. After Sonia chastises Neha regarding Jai's actions, she then falls for him too. Sonia, who’s secretly in love with Jai, becomes heartb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Affinity Constant
The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical equilibrium, a state approached by a dynamic chemical system after sufficient time has elapsed at which its composition has no measurable tendency towards further change. For a given set of reaction conditions, the equilibrium constant is independent of the initial analytical concentrations of the reactant and product species in the mixture. Thus, given the initial composition of a system, known equilibrium constant values can be used to determine the composition of the system at equilibrium. However, reaction parameters like temperature, solvent, and ionic strength may all influence the value of the equilibrium constant. A knowledge of equilibrium constants is essential for the understanding of many chemical systems, as well as the biochemical processes such as oxygen transport by hemoglobin in blood and acid–base homeostasis in the human body. Stability constants, formation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Analytical Chemistry
Analytical skill, Analytical chemistry studies and uses instruments and methods to Separation process, separate, identify, and Quantification (science), quantify matter. In practice, separation, identification or quantification may constitute the entire analysis or be combined with another method. Separation isolates analytes. Qualitative inorganic analysis, Qualitative analysis identifies analytes, while Quantitative analysis (chemistry), quantitative analysis determines the numerical amount or concentration. Analytical chemistry consists of classical, wet chemistry, wet chemical methods and modern analytical techniques. Classical qualitative methods use separations such as Precipitation (chemistry), precipitation, Extraction (chemistry), extraction, and distillation. Identification may be based on differences in color, odor, melting point, boiling point, solubility, radioactivity or reactivity. Classical quantitative analysis uses mass or volume changes to quantify amount. Ins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Methods
Protein methods are the techniques used to study proteins. There are experimental methods for studying proteins (e.g., for detecting proteins, for isolating and purifying proteins, and for characterizing the structure and function of proteins, often requiring that the protein first be purified). Computational methods typically use computer programs to analyze proteins. However, many experimental methods (e.g., mass spectrometry) require computational analysis of the raw data. Genetic methods Experimental analysis of proteins typically requires expression and purification of proteins. Expression is achieved by manipulating DNA that encodes the protein(s) of interest. Hence, protein analysis usually requires DNA methods, especially cloning. Some examples of genetic methods include conceptual translation, Site-directed mutagenesis, using a fusion protein, and matching allele with disease states. Some proteins have never been directly sequenced, however by translating codons from known ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Taylor Dispersion
Taylor dispersion or Taylor diffusion is an apparent or effective diffusion of some scalar field arising on the large scale due to the presence of a strong, confined, zero-mean shear flow on the small scale. Essentially, the shear acts to smear out the concentration distribution in the direction of the flow, enhancing the rate at which it spreads in that direction. The effect is named after the British fluid dynamicist G. I. Taylor, who described the shear-induced dispersion for large Peclet numbers. The analysis was later generalized by Rutherford Aris for arbitrary values of the Peclet number, and hence the process is sometimes also referred to as Taylor-Aris dispersion. The canonical example is that of a simple diffusing species in uniform Poiseuille flow through a uniform circular pipe with no-flux boundary conditions, but is relevant in many other contexts, including the spread of pollutants in rivers and of drugs in blood flow and rivulet flow. Description We use ''z'' as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mass Diffusivity
Diffusivity, mass diffusivity or diffusion coefficient is usually written as the proportionality constant between the molar flux due to molecular diffusion and the negative value of the gradient in the concentration of the species. More accurately, the diffusion coefficient times the local concentration is the proportionality constant between the negative value of the mole fraction gradient and the molar flux. This distinction is especially significant in gaseous systems with strong temperature gradients. Diffusivity derives its definition from Fick's law and plays a role in numerous other equations of physical chemistry. The diffusivity is generally prescribed for a given pair of species and pairwise for a multi-species system. The higher the diffusivity (of one substance with respect to another), the faster they diffuse into each other. Typically, a compound's diffusion coefficient is ~10,000× as great in air as in water. Carbon dioxide in air has a diffusion coefficient of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Quaternary Structure
Protein quaternary structure is the fourth (and highest) classification level of protein structure. Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits). Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits. In contrast to the first three levels of protein structure, not all proteins will have a quaternary structure since some proteins function as single units. Protein quaternary structure can also refer to biomolecular complexes of proteins with nucleic acids and other cofactors. Description and examples Many proteins are actually assemblies of multiple polypeptide chains. The quaternary structure refers to the number and arrangement of the protein subunits w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Blood Plasma
Blood plasma is a light Amber (color), amber-colored liquid component of blood in which blood cells are absent, but which contains Blood protein, proteins and other constituents of whole blood in Suspension (chemistry), suspension. It makes up about 55% of the body's total blood volume. It is the Intravascular compartment, intravascular part of extracellular fluid (all body fluid outside cells). It is mostly water (up to 95% by volume), and contains important dissolved proteins (6–8%; e.g., serum albumins, globulins, and fibrinogen), glucose, clotting factors, electrolytes (, , , , , etc.), hormones, carbon dioxide (plasma being the main medium for excretory product transportation), and oxygen. It plays a vital role in an intravascular osmotic effect that keeps electrolyte concentration balanced and protects the body from infection and other blood-related disorders. Blood plasma can be separated from whole blood through blood fractionation, by adding an anticoagulant to a tube ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nanoparticle
A nanoparticle or ultrafine particle is a particle of matter 1 to 100 nanometres (nm) in diameter. The term is sometimes used for larger particles, up to 500 nm, or fibers and tubes that are less than 100 nm in only two directions. At the lowest range, metal particles smaller than 1 nm are usually called atom clusters instead. Nanoparticles are distinguished from microparticles (1-1000 μm), "fine particles" (sized between 100 and 2500 nm), and "coarse particles" (ranging from 2500 to 10,000 nm), because their smaller size drives very different physical or chemical properties, like colloidal properties and ultrafast optical effects or electric properties. Being more subject to the Brownian motion, they usually do not sediment, like colloid, colloidal particles that conversely are usually understood to range from 1 to 1000 nm. Being much smaller than the wavelengths of visible light (400-700 nm), nanoparticles cannot be seen with ordinary ... [...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] |
