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Polarizability increases down on columns of the periodic table. [9] Likewise, larger molecules are generally more polarizable than smaller ones. Water is a very polar molecule, but alkanes and other hydrophobic molecules are more polarizable. Water with its permanent dipole is less likely to change shape due to an external electric field.
However, because water is a polar molecule this process of simple diffusion is relatively slow, and in tissues with high water permeability the majority of water passes through aquaporin. [ 4 ] [ 5 ] The 2003 Nobel Prize in Chemistry was awarded jointly to Peter Agre for the discovery of aquaporins [ 6 ] and Roderick MacKinnon for his work on ...
where 2.60 is the correction for the oxidative dimerization of water, obtained from a least-squares correlation of data in Edwards’ first paper on the subject. [1] α and β are then parameters unique to specific nucleophiles that relate the sensitivity of the substrate to the basicity and polarizability factors. [6]
where μ is the electric dipole moment of the effectively polarized water molecule (2.35 D for the SPC/E model), μ 0 is the dipole moment of an isolated water molecule (1.85 D from experiment), and α i is an isotropic polarizability constant, with a value of 1.608 × 10 −40 F·m 2. Since the charges in the model are constant, this ...
The folding funnel hypothesis is closely related to the hydrophobic collapse hypothesis, under which the driving force for protein folding is the stabilization associated with the sequestration of hydrophobic amino acid side chains in the interior of the folded protein. This allows the water solvent to maximize its entropy, lowering the total ...
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]
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 ...