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In colloidal chemistry, one property of a lipid bilayer is the relative mobility (fluidity) of the individual lipid molecules and how this mobility changes with temperature. This response is known as the phase behavior of the bilayer. Broadly, at a given temperature a lipid bilayer can exist in either a liquid or a solid phase.
When the membrane potential of a cell goes for a long period of time without changing significantly, it is referred to as a resting potential or resting voltage. This term is used for the membrane potential of non-excitable cells, but also for the membrane potential of excitable cells in the absence of excitation.
Electrochemical energy is one of the many interchangeable forms of potential energy through which energy may be conserved. It appears in electroanalytical chemistry and has industrial applications such as batteries and fuel cells. In biology, electrochemical gradients allow cells to control the direction ions move across membranes.
Illustration of a eukaryotic cell membrane Comparison of a eukaryotic vs. a prokaryotic cell membrane. The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a cell from the outside environment (the extracellular space).
Peter D. Mitchell proposed the chemiosmotic hypothesis in 1961. [1] In brief, the hypothesis was that most adenosine triphosphate (ATP) synthesis in respiring cells comes from the electrochemical gradient across the inner membranes of mitochondria by using the energy of NADH and FADH 2 formed during the oxidative breakdown of energy-rich molecules such as glucose.
Two experiments in 1925 laid the groundwork to fill in this gap. By measuring the capacitance of erythrocyte solutions, Hugo Fricke determined that the cell membrane was 3.3 nm thick. [111] Although the results of this experiment were accurate, Fricke misinterpreted the data to mean that the cell membrane is a single molecular layer. Prof. Dr.
The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. [19] The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. [3]
Thermodynamically the flow of substances from one compartment to another can occur in the direction of a concentration or electrochemical gradient or against it. If the exchange of substances occurs in the direction of the gradient, that is, in the direction of decreasing potential, there is no requirement for an input of energy from outside the system; if, however, the transport is against ...