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Hofmeister Series
The Hofmeister series or lyotropic series is a classification of ions in order of their lyotrophic properties, which is the ability to salt out or salt in proteins. The effects of these changes were first worked out by Franz Hofmeister, who studied the effects of cations and anions on the solubility of proteins. Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and (it was discovered later) on the stability of their secondary and tertiary structure. Anions appear to have a larger effect than cations, and are usually ordered : \mathrm (This is a partial listing; many more salts have been studied.) The order of cations is usually given as : \mathrm The mechanism of the Hofmeister series is not entirely clear, but does not seem to result from changes in general water structure, instead more specific interactions between ions and proteins and ions and the water molecules directly contacting the proteins may be more important. Re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prag Medizinische Fakultät Franz Hofmeister 448
Prag may refer to: * German, Swedish, Danish, Icelandic and Turkish for Prague * Adi Prag (born 1957), Israeli Olympic swimmer *Derek Prag (1923–2010), British politician *Rameshbabu Praggnanandhaa Rameshbabu Praggnanandhaa (born 10 August 2005) is an Indian chess grandmaster. A chess prodigy, he earned the international master title at the age of 10, the youngest at the time to do so, and the grandmaster title at age 12, the second-yo ... (born 2005), Indian chess player * ''Prague'' (2006 film), Danish film starring Mads Mikkelsen, Stine Stengade and Jana Plodková {{disambiguation, surname ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrophobic Effect
The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules. The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes hydrogen bonding between molecules of water and minimizes the area of contact between water and nonpolar molecules. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute. A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity. The hydrophobic effect is responsible for the separation of a mixture of oil and water into its two components. It is also responsible for effects related to biology, including: cell membrane and vesicle formation, protein folding, insertion of membrane proteins into the nonpolar lipid environment and protein- small molecule associations. Hence th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Solutions
Solution may refer to: * Solution (chemistry), a mixture where one substance is dissolved in another * Solution (equation), in mathematics ** Numerical solution, in numerical analysis, approximate solutions within specified error bounds * Solution, in problem solving * Solution, in solution selling Other uses * V-STOL Solution, an ultralight aircraft * Solution (band), a Dutch rock band ** ''Solution'' (Solution album), 1971 * Solution A.D. Solution A.D. was an American rock band from East Stroudsburg, Pennsylvania. The band was initially named Solution, and appended the "A.D." after discovering that another group with the same name already existed. Solution A.D.at Allmusic The gr ..., an American rock band * ''Solution'' (Cui Jian album), 1991 * ''Solutions'' (album), a 2019 album by K.Flay See also * The Solution (other) * {{disambiguation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ionic Strength
The ionic strength of a solution is a measure of the concentration of ions in that solution. Ionic compounds, when dissolved in water, dissociate into ions. The total electrolyte concentration in solution will affect important properties such as the dissociation constant or the solubility of different salts. One of the main characteristics of a solution with dissolved ions is the ionic strength. Ionic strength can be molar (mol/L solution) or molal (mol/kg solvent) and to avoid confusion the units should be stated explicitly. The concept of ionic strength was first introduced by Lewis and Randall in 1921 while describing the activity coefficients of strong electrolytes. Quantifying ionic strength The molar ionic strength, ''I'', of a solution is a function of the concentration of ''all'' ions present in that solution. :I = \begin\frac\end\sum_^ c_i z_i^ where one half is because we are including both cations and anions, ''c''i is the molar concentration of ion i (M, mol ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Denaturation (biochemistry)
In biochemistry, denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein denaturation is also a consequence of cell death. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility to aggregation due to the exposure of hydrophobic groups. The loss of solubility as a result of denaturation is called ''coagulation''. Denatured proteins lose their 3D structure and therefore cannot function. Protein folding is key to whether a globular or membrane protein can do its job correctly; it mu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chemical Equilibrium
In a chemical reaction, chemical equilibrium is the state in which both the Reagent, reactants and Product (chemistry), products are present in concentrations which have no further tendency to change with time, so that there is no observable change in the properties of the system. This state results when the forward reaction proceeds at the same rate as the Reversible reaction, reverse reaction. The reaction rates of the forward and backward reactions are generally not zero, but they are equal. Thus, there are no net changes in the concentrations of the reactants and products. Such a state is known as dynamic equilibrium. Historical introduction The Concept learning, concept of chemical equilibrium was developed in 1803, after Claude Louis Berthollet, Berthollet found that some chemical reactions are Reversible reaction, reversible. For any reaction mixture to exist at equilibrium, the reaction rate, rates of the forward and backward (reverse) reactions must be equal. In the fo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribonuclease A
Pancreatic ribonuclease family (, ''RNase'', ''RNase I'', ''RNase A'', ''pancreatic RNase'', ''ribonuclease I'', ''endoribonuclease I'', ''ribonucleic phosphatase'', ''alkaline ribonuclease'', ''ribonuclease'', ''gene S glycoproteins'', ''Ceratitis capitata alkaline ribonuclease'', ''SLSG glycoproteins'', ''gene S locus-specific glycoproteins'', ''S-genotype-assocd. glycoproteins'', ''ribonucleate 3'-pyrimidino-oligonucleotidohydrolase'') is a superfamily of pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomono nucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the RNA helix by complexing with single-stranded RNA; the complex arises by an extended multi-site cation-anion interaction between lysine and arginine residues of the enzyme and phosphate groups of th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ammonium Sulfate Precipitation
Ammonium sulfate precipitation is one of the most commonly used methods for large and laboratory scale protein purification and fractionation that can be used to separate proteins by altering their solubility in the presence of a high salt concentration. Properties Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium () and sulfate () in aqueous solutions. Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive. Mechanism Ammonium sulfate, as well as other neutral salts, will stabilize proteins by preferential solvation. Proteins are usually stored in ammonium sulfate because it inhibits bacterial growth. With the addition of ammonium sulfate, proteins unfolded by denaturants can be pushed into their native conformations. This can be seen with the folding of recombinant proteins. The solubility ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Purification
Protein purification is a series of processes intended to isolate one or a few proteins from a complex mixture, usually cells, tissues or whole organisms. Protein purification is vital for the specification of the function, structure and interactions of the protein of interest. The purification process may separate the protein and non-protein parts of the mixture, and finally separate the desired protein from all other proteins. Ideally, to study a protein of interest, it must be separated from other components of the cell so that contaminants won't interfere in the examination of the protein of interest's structure and function. Separation of one protein from all others is typically the most laborious aspect of protein purification. Separation steps usually exploit differences in protein size, physico-chemical properties, binding affinity and biological activity. The pure result may be termed protein isolate. Purpose The protein manufacturing cost remains high and there is a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
London South Bank University
London South Bank University (LSBU) is a public university in Elephant and Castle, London. It is based in the London Borough of Southwark, near the South Bank of the River Thames, from which it takes its name. Founded in 1892 as the Borough Polytechnic Institute, it achieved university status in 1992 under the Further and Higher Education Act 1992. In September 2003, the university underwent its most recent name change to become London South Bank University (LSBU) and has since opened several new centres including the School of Health and Social Care, the Centre for Efficient and Renewable Energy in Buildings (CEREB), a new Student Centre, an Enterprise Centre, and a new media centre Elephant Studios. The university has students and 1,700 staff. In November 2016, the university was named the Entrepreneurial University of the Year at the Times Higher Education Awards. In the inaugural 2017 Teaching Excellence Framework, London South Bank University was awarded a Silver rati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrophobic Interaction
In chemistry, hydrophobicity is the physical property of a molecule that is seemingly repelled from a mass of water (known as a hydrophobe). In contrast, hydrophiles are attracted to water. Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle. Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. Hydrophobic is often used interchangeably with lipophilic, "fat-loving". However, the two terms are not synonymous. While hydrophobic substances are usually lipophilic, there are exceptions ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
