An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
Electron Transport Chain
The electron transport chain, also known as the electron transport system, is a group of proteins that transfer electrons through a membrane within mitochondria to create a gradient of protons that drives adenosine triphosphate (ATP)synthesis. The cell uses ATP as an energy source for metabolic processes and cellular functions. ETC involves series of reactions that convert redox energy from NADH (nicotinamide adenine dinucleotide (NAD) + hydrogen (H)) and FADH2(flavin adenine dinucleotide (FAD)) oxidation into proton-motive force(PMF), which is then used to synthesize ATP through conformational changes in the ATP synthase complex, a process known as oxidative phosphorylation.
Metabolism
Picture a campfire. It keeps the body warm on a cold night and provides light. To ensure that the fire keeps burning, fuel needs to be added(pieces of wood in this case). When a small piece is added, the fire burns bright for a bit and then dies down unless more wood is added. But, if too many pieces are placed at a time, the fire escalates and burns for a longer time, without actually burning away all the pieces that have been added. Many of them, especially the larger chunks or damp pieces, remain unburnt.
Cellular Respiration
Cellular respiration is the cellular process involved in the generation of adenosine triphosphate (ATP) molecules from the organic nutritional source obtained from the diet. It is a universal process observed in all types of life forms. The glucose (chemical formula C6H12O6) molecules are the preferred raw material for cell respiration as it possesses a simple structure and is highly efficient in nature.
An antibody binds to another protein with an
equilibrium constant, K, of 5 × 109 M–1. When it binds to
a second, related protein, it forms three fewer hydrogen
bonds, reducing its binding affinity by 11.9 kJ/mole. What
is the K for its binding to the second protein? (Free-energy
change is related to the equilibrium constant by the equa-
tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)
and T is 310 K.)
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