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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 ...
An important concept related to the equilibrium potential is the driving force. Driving force is simply defined as the difference between the actual membrane potential and an ion's equilibrium potential V m − E i {\displaystyle V_{\mathrm {m} }-E_{\mathrm {i} }\ } where E i {\displaystyle E_{\mathrm {i} }\ } refers to the equilibrium ...
The constitutive equations describe how the quantity in question responds to various stimuli via transport. Prominent examples include Fourier's law of heat conduction and the Navier–Stokes equations , which describe, respectively, the response of heat flux to temperature gradients and the relationship between fluid flux and the forces ...
In physical chemistry, the Evans–Polanyi principle (also referred to as the Bell–Evans–Polanyi principle, Brønsted–Evans–Polanyi principle, or Evans–Polanyi–Semenov principle) observes that the difference in activation energy between two reactions of the same family is proportional to the difference of their enthalpy of reaction.
A force field is used to minimize the bond stretching energy of this ethane molecule.. Molecular mechanics uses classical mechanics to model molecular systems. The Born–Oppenheimer approximation is assumed valid and the potential energy of all systems is calculated as a function of the nuclear coordinates using force fields.
Part of force field of ethane for the C-C stretching bond. In the context of chemistry, molecular physics, physical chemistry, and molecular modelling, a force field is a computational model that is used to describe the forces between atoms (or collections of atoms) within molecules or between molecules as well as in crystals.
In statistical mechanics, the Zimm–Bragg model is a helix-coil transition model that describes helix-coil transitions of macromolecules, usually polymer chains. Most models provide a reasonable approximation of the fractional helicity of a given polypeptide; the Zimm–Bragg model differs by incorporating the ease of propagation (self-replication) with respect to nucleation.
Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, [8] [9] [10] although formation of hydrogen bonds within the protein also stabilizes protein structure. [11] [12]