Unit Six/Eight: Metabolism And Energy And Immunity Flashcards
(92 cards)
Conservation of energy
Energy cannot be created or destroyed, but it can be changed from one form to another
What are the forms and types of energy?
Potential or stored energy
Kinetic or energy in motion
Second law of thermodynamics
Every energy transformation makes the universe less organized and more disordered
Heat
The energy if random molecular movement in which half of energy is lost as
Entropy
Used to indicate the relative amount of disorganization
Metabolism
All the chemical reactions that occur in a cell. They can be divided into catabolism and anabolism
Catabolism
Breaking down reactions
Anabolism
Building reactions
Free energy
(G) the amount of energy available or still free to do the work
How is the change in free energy calculated?
By subtracting the free energy content of the reactants from that of the products
Exergonic reactions
(- change G)?energy released, occurs spontaneously
Endergonic reactions
(+ change G) products have more free energy than the reactants with an input of energy
Coupled reactions
Exergonic reactions is used to drive endergonic reactions
Activation energy
Energy that must be added to cause molecules to react with one another
What lowers activation energy?
Catalysts
Structure of an enzyme
Protein molecules that put stress on chemical bonds, lower activation energy required to speed up chemical reactions
Active site
Globular proteins that have a depression
Substrate
Molecule an enzyme acts on
What factors effect enzyme activity?
Temperature, ph, substrate concentration,enzyme concentration
Temperature affecting enzymes
Too cold creates a rigid bond with no induced fit and too jot denatures an enzyme when the peptide bond fails
Ph affecting an enzyme
Too extreme denatures an enzyme
Substrate concentration affecting an enzyme
Reaction rate will level off as substrate is available
Enzyme concentration affecting an enzyme
Reaction rate increases until all enzyme is used
No competitive inhibition
Binding of a inhibitor at a site outside of the active site changes the shape of the enzyme (allosteric change) so that substrate can’t bind to the enzyme. Product inhibits enzyme which creates it