wayground logo

Free Printable Worksheets

Font size

S
M
L
XL
Worksheets

Biochem Exam I_Fall 2022: Max and Serena

Total questions: 41

Worksheet time: 23mins

Name
Class
Date
1.

Which is Not considered an evolutionary life kingdom?

a)

Animalia

b)

Protista

c)

Plantae

d)

Bacteria

e)

Trick question: all of the previous choices are kingdoms

2.

Depending on their source of energy, organisms can be

a)

chemoautotrophs or chemoheterotrophs

b)

Chemotrophs or phototrophs

c)

Chemoheterotrophs and photoheterotrophs

d)

Photoautotrophs and chemoautotrophs

3.

Which is NOT an accurate statement?

a)

All cells have a plasma membrane

b)

All living organisms are in a dynamic steady state far from equilibrium

c)

The ribosome is solely a eukaryotic organelle

d)

Living cells exchange matter and energy with their surroundings

4.

Supramolecular structures in the cell are often held together by

a)

Covalent interactions

b)

Non-covalent interactions

5.

Water has several interesting properties that support life. Which ones are they? Check all that apply.

a)

Cohesiveness

b)

Adhesiveness

c)

Low specific heat

d)

Higher density of ice compared to liquid water

6.

Hydrogen bonds are unique to water.

a)

True

b)

False

7.

Water has a smaller dielecteric constant than most hydrophobic solvents. This is why water is able to dissolve salts.

a)

True

b)

False

8.

Whic is the true statement? In the context of water...

a)

Ionic bonds are stronger than covalent bonds

b)

Hydrogen Bonds are weaker than Van der Waals interactions

c)

Ionic bonds are weaker than covalent bonds

9.

Which of these are colligative properties? Check all that apply

a)

Surface tension

b)

Boiling point

c)

Color

d)

Osmolarity

e)

Melting point

10.

Blood pH is maintained in the normal range by the bicarbonate buffer system.

a)

True

b)

False

11.

Which of the pairs below show the correct amino acid name and single letter code (select all that apply)?

a)

Tyrosine- Y

b)

Arginine- R

c)

Glutamine- Q

d)

Alanine- A

e)

Tryptophan- W

12.

All amino acids are alpha-amino acids and have common backbone elements. Which is Not a common backbone component of an amino acid?

a)

Amino group

b)

Carboxylic group

c)

Hydroxyl group

d)

Central alpha -carbon

13.

Which of these amino acid and R groups are associated incorrectly?

a)

V---- Aliphatic Group

b)

E---- Acidic Group

c)

Q----Basic Group

d)

F----Polar Group

14.

Which of the following amino acids has a net negative charge at physiologic pH (~7.4)?

a)

Glutamic acid

b)

Histidine

c)

Lysine

d)

Asparagine

15.

Amino acids found in hemoglobin (or any other protein) uniformly have which configuration?

a)

L

b)

R

c)

S

d)

D

16.

Gel-filtration chromatography separates on the basis of...

a)

Size and Shape

b)

Net charge

c)

Affinity

d)

How cool you are

17.

You are attempting to isolate Protein A from a patient sample that contains several proteins. Protein A has a molecular weight of 50 kDa and has a distinct charge at lower pH. What technique could best isolate Protein A?

a)

Edman Degradation

b)

Size Exclusion Chromatography

c)

Affinity Binding Chromatography

d)

SDS-PAGE and isoelectric focusing

18.

 Which of these amino acids would you expect to find in the core of a protein? (Check all that apply)

a)

L

b)

K

c)

V

d)

F

e)

Q

19.

The enzyme chymotrypsin only targets the bond on the C-side of amino acids with aromatic R-Groups. Which of the following peptides can chymotrypsin cleave? The sequences are written starting at the N-terminal to the C-Terminal.

a)

G-A-K-L-L-L-F

b)

P-I-G-Y-G-G-Q

c)

G-L-A-D-D-A-D

d)

A-V-I-L-L-I-L

20.

What is the PI of this amino acid? What is the identity of the Amino Acid (Check 2 answers)

a)

PI=10.75

b)

PI=5.55

c)

PI=7

d)

Aspartic Acid

e)

Arginine

21.

When an amino acid is at a pH below its pI value, the amino acid has a net positive charge.

a)

True

b)

False

22.

If you add a mixture of proteins into a cation exchange column, what would you expect to elute out first if you use a neutral mobile phase?

a)

Proteins high in basic amino acids

b)

Positively Charged Proteins

c)

Negatively Charged Proteins

d)

None of the proteins would elute

23.

Which of these statements about Keratin is False?

a)

The super-twisted coiled-coil structure is left-handed

b)

Keratin fibers form intermediate filaments

c)

Keratin is composed of hydrophilic amino acids

d)

Individual keratin chains are right-handed alpha-helices

24.

Which of the following properties of a protein is least likely to be affected by changes in pH?

a)

Primary Structure

b)

Secondary Structure

c)

Tertiary Structure

d)

Net Charge

25.

Which of the following can stabilize protein structures? (Check all that apply)

a)

Salt Bridges

b)

Disulfide Bonds

c)

Hydrophobic Effect

d)

Hydrogen Bonds

e)

Chaperone Proteins

26.

How are secondary structures stabilized?

a)

Hydrogen bonds between polar R-Groups

b)

Ionic interaction between carbonyl backbone and R-Groups

c)

Hydrogen bonds between acidic and basic R-Grou

d)

Hydrogen bonds between carbonyl oxygen and amide groups

e)

These structures do not stabilize proteins

27.

You denature a pure enzyme sample using urea and a reducing agent. You observe no activity when the substrate is added, however, once the added reagents are removed there is a return in enzymatic activity. Which of the statements is true?

a)

The enzyme does not have disulfide bonds

b)

The enzyme does not require a chaperone to fold properly

c)

The folding is random

d)

The protein's structure is not vital to its enzymatic function

28.

The cytoskeleton component filamentous actin is made of many subunits, all of which are globular actin. Which term refers to globular actin in this context?

a)

Prosthetic group

b)

Protomer

c)

Ligand

d)

Cofactor

e)

polymorphism

29.

A higher Kd indicates a higher affinity for the protein to bind to the ligand.

a)

True

b)

False

30.

In Hemoglobin, T is the low affinity state.

a)

True

b)

False

31.

2. BPG helps in low oxygen environments by binding to hemoglobin and increasing its affinity to oxygen.

a)

True

b)

False

32.

The binding of oxygen to hemoglobin is an example of cooperative binding.

a)

So true, so true

b)

Nah bro, that's false

33.

Which of these statements about Enzymes are true? (choose all that apply)

a)

Enzymes increase the amount of free energy in a reaction

b)

Enzymes are not regulated within cells

c)

Enzymes increase the rate of reactions

d)

Enzymes increase the amount of activation in order to increase the rate of reaction

e)

Enzymes are able to catalyze several reactions without being degraded

34.

 Based of this graph, where, in the reaction progression, would an enzyme directly affect the reaction? How would it affect the reaction? (Select all that apply)

a)

A and C

b)

B

c)

Lower the activation energy

d)

Destabilize the transition state of the substrate

e)

Make the reaction spontaneous

35.

Which of these statements are true? check all that apply.

a)

With enzymes, specificity for substrate is lowered

b)

Enzymes allow for product formation regulation

c)

Most enzymes are globular proteins

d)

The binding energy between the enzyme and the substrate helps lower the activation energy

36.

A low Km value indicate a high affinity for the substrate.

a)

True

b)

False

37.

The standard free energy of a reaction is not affected by the Keq

a)

True

b)

False

38.

In the lineweaver-Burk linear plot,

a)

Km/Vmax is the y-intercept of the curve

b)

1/Vmax is the x-intercept

c)

Km/Vmax is the slope

d)

Vmax/Km is the slope

39.

Enzymes that exhibits allosterism

a)

Obey Michealis -Menten kinetics

b)

Are subject to conformational change upon binding of a modulator

40.

Which statements are Not true?

a)

The sequential and pingpong mechanisms can be distinguished easily using the Lineweaver-Burk plot

b)

Competitive inhibitors affect the Vmax of the reaction

c)

Non-competitive inhibitors increase the Vmax and decrease the Km

d)

Toxins often cause reversible inhibition of enzymes

e)

Competitive inhibitors are a type of mixed inhibitors

41.

In terms of regulation,...

a)

Oxygen can be considered a homotropic allosteric regulator of hemoglobin

b)

Phosphorylation is the most common non-covalent modification for enzyme regulation