Chapter 10: Proteins, Amino Acids, Enzymes, Peptides

Question 1

What are the 10 essential amino acids

Answer 1

Arginine
Histidine
Isoleucine

Leucine
Lysine
Methionine

Phenylalanine
Threonine
Tryptophan
Valine

Question 2

What are the 10 non essential amino acids

Answer 2

Alanine
Asparagine
Aspartate

Cysteine
Glutamate
Glutamine

Glycine
Proline
Serine
Tyrosine

Question 3

What are essential amino acids?

Answer 3

Essential amino acids cannot be made by the body. (must get from food)

Question 4

What are non essential amino acids

Answer 4

our bodies can produce the amino acid, even if we do not get it from the food we eat.

Question 5

what is an amino acid structure?

Answer 5

central carbon atom with -COOH,-H2N, and a R group
So
H
|
H2N—C—COOH
|
R group

Question 6

What is the acid base nature of amino acids

Answer 6

Amino acids can function as both Bronsted-Lowry acids and bases because they have both acidic and basic functional groups

Question 7

What is a Bronsted-Lowry acid?

Answer 7

any species that can donate a proton

Question 8

What is a Bronsted-Lowry base?

Answer 8

Anything that can accept a proton

Question 9

What is the isoelectric point?

Answer 9

is the pH at which a molecule has a net charge of zero

Question 10

How do you find the net charge?

Answer 10

Subtract protons and electrons

Question 11

How do you know the atomic number?

Answer 11

The number of protons

Question 12

What is the mass number?

Answer 12

Protons+neutrons

Question 13

The zwitterion of an amino acid exists at a pH _____ to the isoelectric point

Answer 13

The zwitterion of an amino acid exists at a pH equal to the isoelectric point

Question 14

Amide bond condensation reaction is when

Answer 14

The −OH from the carboxyl group of one amino acid combines with a hydrogen atom from the amine group of the other amino acid to produce water

Question 15

what is an example of an Amide bond condensation reaction

Answer 15

when ethanol is heated in the presence of sulfuric acid, diethyl ether and water are formed:

Question 16

What is the N terminus?

Answer 16

H2N-CH-C
the first part of the protein that exits the ribosome during protein biosynthesis

Question 17

What is the C terminus

Answer 17

C-OH
the end of an amino acid chain

Question 18

what are the 4 levels of the 3D structure of proteins

Answer 18

primary, secondary, tertiary, and quaternary structure.

Question 19

What is the primary structure of proteins

Answer 19

sequence of a chain of amino acids (Looks like a long snake)

Question 20

What is the secondary structure of proteins

Answer 20

hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern. (Looks like folded paper)

Question 21

What is the tertiary structure of proteins

Answer 21

Three dimensional folding pattern of a protein due to side chain interactions (looks like the snake is laying onto of itself)

Question 22

What is the quaternary structure of proteins

Answer 22

Protein consisting of more Than one amino acid chain (Two snakes laying on top of each other)

Question 23

what causes a protein to denature

Answer 23

Heat

Question 24

what causes a protein to renature

Answer 24

when the denaturing influence is removed

Question 25

What is a receptor? What's its function?

Answer 25

-a protein molecule to which substances like hormones, drugs, and antigens can bind. -This allows them to change the activity of a cell

Question 26

What is transporters? What is its function?

Answer 26

-Transporters (membrane transport/carrier proteins) are specialized membrane-spanning proteins - Assist in the movement of ions, peptides, small molecules, lipids and macromolecules across a biological membrane.

Question 27

What is the transportation of oxygen function

Answer 27

-fundamental to aerobic respiration and the survival of organisms through facilitated diffusion

Question 28

what is the antibody function? How do they work?

Answer 28

-protect you when an unwanted substance enters your body -Antibodies bind to these unwanted substances in order to eliminate them from your system.

Question 29

What are enzymes function?

Answer 29

help speed up metabolism, or the chemical reactions in our bodies.

Question 30

What is the active site of an ezyme

Answer 30

The part of the enzyme where the substrate binds

Question 31

What is the substrate of an enzyme

Answer 31

a molecule that an enzyme reacts with at the active site

Question 32

What is the enzyme substrate complex of an enzyme?

Answer 32

an enzyme with its substrate attached at the enzyme's active site

Question 33

What is substrate specificity of an enzyme

Answer 33

The preference of an enzyme for one specific substrate (not all enzyme active sites will accept a substrate)

Question 34

What are The two ES models of enzymes?

Answer 34

-The lock and key model: substrate is the key enzyme is the lock -The induced fit model: enzyme active site changes as well as the substrate to fit

Question 35

How does proximity change enzyme reaction rate

Answer 35

Enzyme proximity effect means the increasing of reaction rate by causing a higher probability of collision when reactants are closer together

Question 36

How does orientation of a substrate change enzyme reaction ?

Answer 36

-the enzyme constrains the substrates into specific reactive conformations, - increases the probability that reactants will collide in the correct orientation to react

Question 37

How does substrate concentration change enzyme reaction rate

Answer 37

At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration

Question 38

How does pH change enzyme reaction rate

Answer 38

Changing the pH outside of this range will slow enzyme activity

Question 39

How does inhibitors change enzyme reaction rate

Answer 39

fewer substrate molecules can bind to the enzymes so the reaction rate is decreased.

Question 40

What are the 3 types of enzyme inhibitors

Answer 40

-Competitive Inhibition: binds to the active site and prevents the substrate from binding there. -Non-competitive Inhibition: binds to a different site on the enzyme; it doesn't block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently. -Uncompetitive Inhibition: when an inhibitor binds to an allosteric site of a enzyme, but only when the substrate is already bound to the active site.

Question 41

The structure of glycine

Answer 41

...................................H | HO2CCH2NH2 (H2N-C-COOH) | H

Question 42

The structure of alanine

Answer 42

.........H | (NH2-C-COOH) | CH3

Question 43

The structure of serine

Answer 43

COOH | H2N-C-H | CH2OH

Question 44

The structure of lysine

Answer 44

COOH | H2N-C-H | CH2 | CH2 | CH2 | CH2 | NH2

Question 45

The structure of aspartic acid

Answer 45

COOH | H2N-C-H | CH2 | COOH