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Pressure Perturbation Calorimetry
Pressure perturbation calorimetry (PPC) is a technique closely related to isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC). In brief, PPC measures heat changes associated with dilute aqueous solutions of proteins or other biomolecules in response to introduction of relatively small pressure perturbations (± 5 atm). Importantly, such heat changes can be related to thermodynamic properties of proteins such as hydration and conformational transitions upon folding and/or ligand binding. See also * Differential scanning calorimetry * Isothermal microcalorimetry * Isothermal titration calorimetry Isothermal titration calorimetry (ITC) is a physical technique used to determine the thermodynamic parameters of interactions in solution. It is most often used to study the binding of small molecules (such as medicinal compounds) to larger macro ... * Sorption calorimetry Bibliography * * * {{refend Calorimetry ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isothermal Titration Calorimetry
Isothermal titration calorimetry (ITC) is a physical technique used to determine the thermodynamic parameters of interactions in solution. It is most often used to study the binding of small molecules (such as medicinal compounds) to larger macromolecules (proteins, DNA etc.). It consists of two cells which are enclosed in an adiabatic jacket. The compounds to be studied are placed in the sample cell, while the other cell, the reference cell, is used as a control and contains the buffer in which the sample is dissolved. Thermodynamic measurements ITC is a quantitative technique that can determine the binding affinity (K_a), enthalpy changes (\Delta H), and binding stoichiometry (n) of the interaction between two or more molecules in solution. From these initial measurements, Gibbs free energy changes (\Delta G) and entropy changes (\Delta S) can be determined using the relationship: :::\Delta G = -RT\ln = \Delta H -T\Delta S (where R is the gas constant and T is the absolute ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Differential Scanning Calorimetry
Differential scanning calorimetry (DSC) is a thermoanalytical technique in which the difference in the amount of heat required to increase the temperature of a sample and reference is measured as a function of temperature. Both the sample and reference are maintained at nearly the same temperature throughout the experiment. Generally, the temperature program for a DSC analysis is designed such that the sample holder temperature increases linearly as a function of time. The reference sample should have a well-defined heat capacity over the range of temperatures to be scanned. The technique was developed by E. S. Watson and M. J. O'Neill in 1962, and introduced commercially at the 1963 Pittsburgh Conference on Analytical Chemistry and Applied Spectroscopy. The first adiabatic differential scanning calorimeter that could be used in biochemistry was developed by P. L. Privalov and D. R. Monaselidze in 1964 at Institute of Physics in Tbilisi, Georgia. The term DSC was coined to descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aqueous Solution
An aqueous solution is a solution in which the solvent is water. It is mostly shown in chemical equations by appending (aq) to the relevant chemical formula. For example, a solution of table salt, or sodium chloride (NaCl), in water would be represented as . The word ''aqueous'' (which comes from ''aqua'') means pertaining to, related to, similar to, or dissolved in, water. As water is an excellent solvent and is also naturally abundant, it is a ubiquitous solvent in chemistry. Since water is frequently used as the solvent in experiments, the word solution refers to an aqueous solution, unless the solvent is specified. A ''non-aqueous solution'' is a solution in which the solvent is a liquid, but is not water. (See also Solvent and Inorganic nonaqueous solvent.) Characteristics Substances that are ''hydrophobic'' ('water-fearing') do not dissolve well in water, whereas those that are ''hydrophilic'' ('water-friendly') do. An example of a hydrophilic substance is sodium chlo ... [...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 residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 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 peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biomolecule
A biomolecule or biological molecule is a loosely used term for molecules present in organisms that are essential to one or more typically biological processes, such as cell division, morphogenesis, or development. Biomolecules include large macromolecules (or polyelectrolytes) such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites and natural products. A more general name for this class of material is biological materials. Biomolecules are an important element of living organisms, those biomolecules are often endogenous, produced within the organism but organisms usually need exogenous biomolecules, for example certain nutrients, to survive. Biology and its subfields of biochemistry and molecular biology study biomolecules and their reactions. Most biomolecules are organic compounds, and just four elements—oxygen, carbon, hydrogen, and nitrogen—make up 96% of the human body's mass. But ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Folding
Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a "folded" conformation by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA to a linear chain of amino acids. At this stage the polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding of many proteins begins even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Differential Scanning Calorimetry
Differential scanning calorimetry (DSC) is a thermoanalytical technique in which the difference in the amount of heat required to increase the temperature of a sample and reference is measured as a function of temperature. Both the sample and reference are maintained at nearly the same temperature throughout the experiment. Generally, the temperature program for a DSC analysis is designed such that the sample holder temperature increases linearly as a function of time. The reference sample should have a well-defined heat capacity over the range of temperatures to be scanned. The technique was developed by E. S. Watson and M. J. O'Neill in 1962, and introduced commercially at the 1963 Pittsburgh Conference on Analytical Chemistry and Applied Spectroscopy. The first adiabatic differential scanning calorimeter that could be used in biochemistry was developed by P. L. Privalov and D. R. Monaselidze in 1964 at Institute of Physics in Tbilisi, Georgia. The term DSC was coined to descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isothermal Microcalorimetry
Isothermal microcalorimetry (IMC) is a laboratory method for real-time monitoring and dynamic analysis of chemical, physical and biological processes. Over a period of hours or days, IMC determines the onset, rate, extent and energetics of such processes for specimens in small ampoules (e.g. 3–20 ml) at a constant set temperature (c. 15 °C–150 °C). IMC accomplishes this dynamic analysis by measuring and recording vs. elapsed time the net rate of heat flow (μJ/s = μW) to or from the specimen ampoule, and the cumulative amount of heat (J) consumed or produced. IMC is a powerful and versatile analytical tool for four closely related reasons: # All chemical and physical processes are either exothermic or endothermic—produce or consume heat. # The rate of heat flow is proportional to the rate of the process taking place. # IMC is sensitive enough to detect and follow either slow processes (reactions proceeding at a few % per year) in a few grams of material, or ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isothermal Titration Calorimetry
Isothermal titration calorimetry (ITC) is a physical technique used to determine the thermodynamic parameters of interactions in solution. It is most often used to study the binding of small molecules (such as medicinal compounds) to larger macromolecules (proteins, DNA etc.). It consists of two cells which are enclosed in an adiabatic jacket. The compounds to be studied are placed in the sample cell, while the other cell, the reference cell, is used as a control and contains the buffer in which the sample is dissolved. Thermodynamic measurements ITC is a quantitative technique that can determine the binding affinity (K_a), enthalpy changes (\Delta H), and binding stoichiometry (n) of the interaction between two or more molecules in solution. From these initial measurements, Gibbs free energy changes (\Delta G) and entropy changes (\Delta S) can be determined using the relationship: :::\Delta G = -RT\ln = \Delta H -T\Delta S (where R is the gas constant and T is the absolute ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sorption Calorimetry
The method of sorption calorimetry is designed for studies of hydration of complex organic and biological materials. It has been applied for studies of surfactants, lipids, DNA, nanomaterials and other substances. A sorption calorimetric experiment is performed at isothermal regime, but different temperatures can be studied in separate experiments. In a sorption calorimetric experiment, a two-chamber calorimetric cell is inserted into a double-twin microcalorimeter. Water evaporates, diffuses through the tube connecting two chambers of the calorimetric cell and is absorbed by the studied substance. The amount of evaporated water is calculated from the thermal power registered in the vaporisation chamber: :n_w= \frac From the same data, the activity of water in the sample can also be calculated: :a_w=1-\frac From the thermal powers registered in the two chambers one can calculate the partial molar enthalpy of mixing of water. During the sorption experiment the water content ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
