3

Question 1

ATP is made up of

Answer 1

a nucleotide that consists of a ribose connected to adenine and a chain of 3 phosphate groups

Question 2

energy coupling

Answer 2

the cell harnesses the free energy available using enzymes and catalysts to bring molecules of ATP and reactant molecules of an endergonic reaction closer together

Question 3

The polarity of the proteins is largely dependant on

Answer 3

the side chains of their amino acids which are made up of monomers that make polypetides which can assemble to make a protein

Question 4

How do amino acids connect

Answer 4

with a dehydration reaction, a covalent bonnd between the N of an amino group and a C of the carboxyl group

Question 5

Primary, secondary, tertiary, and quaternary

Answer 5

• amino acids that are combined to make a polypeptide
• twisting of primary in an alpha helix or beta sheet
• three dimensional shape of an individual as it folds on itself

Question 6

enzymes increase the rate of reaction by three ways

Answer 6

• bringing the reacting molecules together
• exposing the reactant molecules to changed charge environments that promote catalysis
• changing the shape of the substrate molecule

Question 7

The rate at which an enzyme can catalyze a reaction can be lowered by

Answer 7

by enzyme inhibitors, which are non-substrate molecules

Question 8

Two mechanisms regulate enzyme activity

Answer 8

• Allosteric Regulation - Allosteric activation- a special molecule binds to another part of the enzyme to change the shape of the active site so the substrate can fit and Allosteric Inihibiton is opposite
• covalent modification

Question 9

What happens in covalent modification

Answer 9

• when you add another molecules to the enzyme to change the activity
• most commonly used with phosphorylation (carried out by protein kinases) and dephosphorylation (carried out by protein phosphatases, the adding and removal of phosphate groups