Microscale Thermophoresis
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Microscale Thermophoresis
Microscale thermophoresis (MST) is a technology for the Biophysics, biophysical analysis of interactions between biomolecules. Microscale thermophoresis is based on the detection of a temperature-induced change in fluorescence of a target as a function of the concentration of a non-fluorescent ligand. The observed change in fluorescence is based on two distinct effects. On the one hand it is based on a temperature related intensity change (TRIC) of the fluorescent probe, which can be affected by binding events. On the other hand, it is based on thermophoresis, the directed movement of particles in a microscopic temperature gradient. Any change of the chemical microenvironment of the fluorescent probe, as well as changes in the solvation shell#Hydration shells of proteins, hydration shell of biomolecules result in a relative change of the fluorescence detected when a temperature gradient is applied and can be used to determine dissociation constant, binding affinities. MST allows me ...
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Thermophoresis
Thermophoresis (also thermomigration, thermodiffusion, the Soret effect, or the Ludwig–Soret effect) is a phenomenon observed in mixtures of mobile particles where the different particle types exhibit different responses to the force of a temperature gradient. This phenomenon tends to move light molecules to hot regions and heavy molecules to cold regions. The term ''thermophoresis'' most often applies to aerosol mixtures whose mean free path \lambda is comparable to its characteristic length scale L, but may also commonly refer to the phenomenon in all phases of matter. The term ''Soret effect'' normally applies to liquid mixtures, which behave according to different, less well-understood mechanisms than gaseous mixtures. Thermophoresis may not apply to thermomigration in solids, especially multi-phase alloys. Thermophoretic force The phenomenon is observed at the scale of one millimeter or less. An example that may be observed by the naked eye with good lighting is when the hot ...
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MST Technology
The Master of Studies or Master in Studies (M.St. or MSt; ) is a postgraduate degree at the University of Oxford, University of Cambridge, University of St Andrews, the Australian National University, University of Dublin and the University of Newcastle (Australia). Depending on the degree, it is comparable to the Master of Arts, Master of Business Administration, Master of Laws, Master of Philosophy, and Master of Science. Its creation was necessitated, in part, by the fact that the Master of Arts degree at Oxford, Cambridge, and Dublin is automatically awarded to graduates after a certain period of time. In contrast, the Master of Studies requires completion of classroom study and a thesis. See also * British degree abbreviations * Master's degree in Europe * Master of Studies in Law * Master of Philosophy The Master of Philosophy (MPhil; Latin ' or ') is a postgraduate degree. In the United States, an MPhil typically includes a taught portion and a significant research po ...
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Enthalpic
Enthalpy , a property of a thermodynamic system, is the sum of the system's internal energy and the product of its pressure and volume. It is a state function used in many measurements in chemical, biological, and physical systems at a constant pressure, which is conveniently provided by the large ambient atmosphere. The pressure–volume term expresses the work (physics), work required to establish the system's physical dimensions, i.e. to make room for it by displacing its surroundings. The pressure-volume term is very small for solids and liquids at common conditions, and fairly small for gases. Therefore, enthalpy is a stand-in for energy in chemical systems; Bond energy, bond, Lattice energy, lattice, solvation and other "energies" in chemistry are actually enthalpy differences. As a state function, enthalpy depends only on the final configuration of internal energy, pressure, and volume, not on the path taken to achieve it. In the International System of Units (SI), the unit ...
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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 know ...
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Biochemistry Methods
The following outline is provided as an overview of and topical guide to biochemistry: Biochemistry – study of chemical processes in living organisms, including living matter. Biochemistry governs all living organisms and living processes. Applications of biochemistry * Testing ** Ames test – salmonella bacteria is exposed to a chemical under question (a food additive, for example), and changes in the way the bacteria grows are measured. This test is useful for screening chemicals to see if they mutate the structure of DNA and by extension identifying their potential to cause cancer in humans. ** Pregnancy test – one uses a urine sample and the other a blood sample. Both detect the presence of the hormone human chorionic gonadotropin (hCG). This hormone is produced by the placenta shortly after implantation of the embryo into the uterine walls and accumulates. ** Breast cancer screening – identification of risk by testing for mutations in two genes&md ...
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Law Of Mass Action
In chemistry, the law of mass action is the proposition that the rate of the chemical reaction is directly proportional to the product of the activities or concentrations of the reactants. It explains and predicts behaviors of solutions in dynamic equilibrium. Specifically, it implies that for a chemical reaction mixture that is in equilibrium, the ratio between the concentration of reactants and products is constant. Two aspects are involved in the initial formulation of the law: 1) the equilibrium aspect, concerning the composition of a reaction mixture at equilibrium and 2) the kinetic aspect concerning the rate equations for elementary reactions. Both aspects stem from the research performed by Cato M. Guldberg and Peter Waage between 1864 and 1879 in which equilibrium constants were derived by using kinetic data and the rate equation which they had proposed. Guldberg and Waage also recognized that chemical equilibrium is a dynamic process in which rates of reaction for t ...
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Diffusion
Diffusion is the net movement of anything (for example, atoms, ions, molecules, energy) generally from a region of higher concentration to a region of lower concentration. Diffusion is driven by a gradient in Gibbs free energy or chemical potential. It is possible to diffuse "uphill" from a region of lower concentration to a region of higher concentration, like in spinodal decomposition. The concept of diffusion is widely used in many fields, including physics (particle diffusion), chemistry, biology, sociology, economics, and finance (diffusion of people, ideas, and price values). The central idea of diffusion, however, is common to all of these: a substance or collection undergoing diffusion spreads out from a point or location at which there is a higher concentration of that substance or collection. A gradient is the change in the value of a quantity, for example, concentration, pressure, or temperature with the change in another variable, usually distance. A change in c ...
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Fluorescence
Fluorescence is the emission of light by a substance that has absorbed light or other electromagnetic radiation. It is a form of luminescence. In most cases, the emitted light has a longer wavelength, and therefore a lower photon energy, than the absorbed radiation. A perceptible example of fluorescence occurs when the absorbed radiation is in the ultraviolet region of the electromagnetic spectrum (invisible to the human eye), while the emitted light is in the visible region; this gives the fluorescent substance a distinct color that can only be seen when the substance has been exposed to UV light. Fluorescent materials cease to glow nearly immediately when the radiation source stops, unlike phosphorescent materials, which continue to emit light for some time after. Fluorescence has many practical applications, including mineralogy, gemology, medicine, chemical sensors (fluorescence spectroscopy), fluorescent labelling, dyes, biological detectors, cosmic-ray detection, vacu ...
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Ligand
In coordination chemistry, a ligand is an ion or molecule (functional group) that binds to a central metal atom to form a coordination complex. The bonding with the metal generally involves formal donation of one or more of the ligand's electron pairs, often through Lewis bases. The nature of metal–ligand bonding can range from covalent to ionic. Furthermore, the metal–ligand bond order can range from one to three. Ligands are viewed as Lewis bases, although rare cases are known to involve Lewis acidic "ligands". Metals and metalloids are bound to ligands in almost all circumstances, although gaseous "naked" metal ions can be generated in a high vacuum. Ligands in a complex dictate the reactivity of the central atom, including ligand substitution rates, the reactivity of the ligands themselves, and redox. Ligand selection requires critical consideration in many practical areas, including bioinorganic and medicinal chemistry, homogeneous catalysis, and environmental chemi ...
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Conformational Change
In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a ''conformational change''. Factors that may induce such changes include temperature, pH, voltage, light in chromophores, concentration of ions, phosphorylation, or the binding of a ligand. Transitions between these states occur on a variety of length scales (tenths of Å to nm) and time scales (ns to s), and have been linked to functionally relevant phenomena such as allosteric signaling and enzyme catalysis. Laboratory analysis Many biophysical techniques such as crystallography, NMR, electron paramagnetic resonance (EPR) using spin label techniques, circular dichroism (CD), hydrogen exchange, and FRET can be used to study macrom ...
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Fluorophore
A fluorophore (or fluorochrome, similarly to a chromophore) is a fluorescent chemical compound that can re-emit light upon light excitation. Fluorophores typically contain several combined aromatic groups, or planar or cyclic molecules with several π bonds. Fluorophores are sometimes used alone, as a tracer in fluids, as a dye for staining of certain structures, as a substrate of enzymes, or as a probe or indicator (when its fluorescence is affected by environmental aspects such as polarity or ions). More generally they are covalently bonded to a macromolecule, serving as a marker (or dye, or tag, or reporter) for affine or bioactive reagents (antibodies, peptides, nucleic acids). Fluorophores are notably used to stain tissues, cells, or materials in a variety of analytical methods, i.e., fluorescent imaging and spectroscopy. Fluorescein, via its amine-reactive isothiocyanate derivative fluorescein isothiocyanate (FITC), has been one of the most popular fluorophores. Fro ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ...
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