Key food molecules

Question 1

zwittierion/ dipolar ion

Answer 1

ion containing an equal number of positive and negative charges.
-amino acids this way due to the amine and carboxyl acid groups (NH3+, COO-)

Question 2

peptide links

Answer 2

carboxyl group and amine group = H2O

this portion then becomes an amide.

Question 3

effect of pH on amino acids

Answer 3

• amino acids are zwitterions

- therefore, it is amphiprotic (acid or base)

Question 4

amino acids basic environment

Answer 4

• acts as an acid.
• due to it losing the H+ when the concentration of H+ ions is lowered.
• NH2 = COO-
• therefore overall negative charge
• anionic form

Question 5

amino acids in acidic environments

Answer 5

• acts as a base
• due to it combining with the increasing concentration of H+.
• COOH= NH3+
• therefore overall positive charge
• cationic form

Question 6

amphoteric

Answer 6

can act as an acid or base

Question 7

formation of proteins

Answer 7

-condensation reactions to for di or poly-peptide bonds. therefore water is released.

Question 8

primary structure

Answer 8

-chain

Question 9

secondary structure

Answer 9

-alpha helix and beta pleated-sheets

Question 10

tertiary structures

Answer 10

• overall three-dimensional structure

- shape depends on the properties of the R group (polarity).

Question 11

Quaternary structure

Answer 11

-two or more polypeptide chains

Question 12

enzymes

Answer 12

provide an alternitive pathway with a lower activation energy.

Question 13

lock-and-key model

Answer 13

the substrate can only react with an enzyme that has a complementary active site. This can be related to a key and a lock, as only a key with a particular shape.

Question 14

induced-fit model

Answer 14

the active site may change tp fit the substrate’s shape.

Question 15

coenzyme what?

Answer 15

organic non-proteins based molecules that assist the enzyme by binding to the active site.
-chemmical structure can change during reaction.

Question 16

temperature on enzymes

Answer 16

cooler temps= not much energy therefore the enzymes move slowly.
high temps= the enzymes denature (the active site is permenantly changed)

Question 17

pH on enzymes

Answer 17

-determines whether the protein acts as an acid or base.

-

Question 18

denaturation

Answer 18

the collapse of intra- and intermolecular bonds that maintian the shape in quaternary, tertiary, and secondary structures of an enzymes, hence altering the ennzymes catalytic activity.

Question 19

hydrolysis of primary vs denaturation

Answer 19

hydrolysis involves the breaking of strong covalent bonds (intramolecular), whereas denaturation involves the breaking of weak intermolecular bonds.