BIOL1007 Lecture Notes - Lecture 5: Enzyme Kinetics, Activation Energy, Endergonic Reaction

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peargoat430

17 Aug 2018

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Hydrophobic interactions drives" the formation of a proteins fold in solution . The change in free energy (ag) is a combination of enthalpy (ah) and entropy (as); The delta h is the total energy in a reaction, the nervous energy (useless energy) needs to be rid off. The contribution of entropy decreases when the temperature is lowered e. g jelly heated and cooled. Because organisms are an open system matter and energy can continually flow in and out of cell. The cell needs lots of free energy to do work so it needs to be far from equilibrium, needs ag to do work. The cell exists inn a steady state that is not at a equilibrium we achieve equilibrium upon death. Steady state is when glucose taken and burn it up to keep in steady stae e. g gym to burn off is different to equilibrium which has diff definition. A negative ag makes reaction thermodynamically favourable.

Related Questions

Protein folding is a thermodynamically favorable process under physiological conditions because:

1- There is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule.

2- No intermediate stage disulphide bonds form during the folding process.

3- There is an increase in entropy associated with protein folding.

4- Of the large negative enthalpy change associated with many noncovalent interactions.

5- All of the above.

limesnake655

Some proteins, once folded âassociateâ to form higher order structures (i.e., quaternary structure). Within these structures the single protein chain is known as a âsubunitâ (not to be confused with a protein domain). If two identical protein chains fold and associate, the quaternary structure is named âhomodimerâ (and the individual subunits are sometimes referred to as âmonomersâ); for three âhomotrimerâ and so on. If, on the other hand, the two protein chains that associate have different primary structures, the quaternary structure is named âheterodimerâ. Using the dimer as an example, we know that the respective regions of the protein subunit surfaces that are interfaced, are responsible for the âfavorable energy of interactionâ which stabilizes the dimeric protein complex.

(a). Although, noncovalent bonding interactions are used both for stabilization of the folded protein molecule and its dimerization, the contribution of the âhydrophobic effectâ to chain folding is significantly greater than its contribution to subunit association. Define the âhydrophobic effectâ and explain why you would expect it to have a more pronounced role in chain folding compared to dimerization of the folded molecules.

(b) As the protein chain folds to the native structure, it loses entropy. Upon dimerization, more protein entropy is lost. Compare and contrast the source of protein entropy loss, which occurs with folding, with that which occurs with dimerization.

redporpoise461

Which intermolecular porcess primarly drives the formation of a bilayer when phospholipids are added to water? Which intermolecular porcess primarly drives the formation of a bilayer when phospholipids are added to water?

A-Lipids cause water to arrange in an ordered, unfavorable cage-like structure.

B-Forcing lipids into a bilayer reduces this effect.

C-The ordered arrangement of a bilayer is more favorable than the disordered state of individual free-floating phospholipids.

D-A bilayer arrangement maximizes the strength of hydrophobic interactions among phospholipids.

E-Phospholipids self-assemble inot a bilayer due to the strong affinity they have for each other.

BIOL1007 Lecture Notes - Lecture 5: Enzyme Kinetics, Activation Energy, Endergonic Reaction

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