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Proteins Questions Flashcards

1
Q

How many amino acids are considered essential?

A

10

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2
Q

CO2 is carried by HbA as?

A

Carbamate

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3
Q

In the Henderson-Hasselbalch equation, if you need the pH of the buffer to be greater than the pKa of the acid that you will use to make the buffer, which of the following will you increase?

A

[Conjugate Base]

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4
Q

BPG stabilizes the “T” form of HbA via what type of interaction?

A

Salt Bridge

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5
Q

When a mutation compromises biologic function of HbA, the condition is termed what?

A

Hemoglobinopathy

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6
Q

When H+ binds to HbA, which form of HbA exists?

A

T Form

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7
Q

What is the oxidation state of Fe in myoglobin & hemoglobin?

A

2+

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8
Q

Which blood protein saturates with O2 at low pressures?

A

Myoglobin

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9
Q

Myoglobin releases O2 to the muscle tissue at which partial pressure of O2?

A

5 mmHg

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10
Q

True or False

Proline can be accommodated on any turn of the alpha-helix.

A

False

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11
Q

When blood glucose enters the RBC, it glycates the pendent chain of which amino acid?

A

Lysine

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12
Q

Primary structures of peptides are stabilized by what?

A

Covalent Peptide Bonds

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13
Q

What type of HbA acts as a buffer?

A

Deoxyhemoglobin

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14
Q

Beta pleated sheets derive their stability from what type of intermolecular force of attraction?

A

Hydrogen Bonds

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15
Q

Myoglobin is rich in what type of secondary structure?

A

Alpha Helicies

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16
Q

Reduced production of a & b subunits of HbA results in what?

A

Alpha & Beta Thalassemia

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17
Q

In the Henderson-Hasselbalch equation, if you need the pH of the buffer to be less than the pKa of the acid that you will use to make the buffer, what will you increase?

A

Molar Concentration of the Acid

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18
Q

Of the two types of beta sheets, in which is the hydrogen bond oriented perpendicular to the backbone of the polypeptide?

A

Antiparallel Beta Sheets

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19
Q

What type of proteins are enzymes?

A

Globular

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20
Q

What joins two adjacent strands of an antiparallel beta sheet?

A

Loops & Bends

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21
Q

What is the p50 value for HbA with O2?

A

26 mmHg

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22
Q

Which amino acid is the precursor to Tyrosine?

A

Phenylalanine

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23
Q

The porphyrin ring around the central Fe atom in Hemoglobin is also called what?

A

Tetrapyrrole

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24
Q

BPG stabilizes which form of hemoglobin?

A

T Form

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25
Q

The interior of myoglobin contains polar or non-polar groups?

A

Non-Polar Groups

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26
Q

What kind of protein is collagen?

A

Fibrous

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27
Q

True or False

pKa values do not depend on the properties of the medium.

28
Q

Electrostative interaction are between what?

A

Positive & Negative Charges within or between Biomolecules

29
Q

What value represents the affinity of Fe2+ in hemoglobin towards CO?

A

~200 times

30
Q

How many amino acids make up the beta chain of hemoglobin?

A

146 Amino Acids

31
Q

Which form of HbA binds to O2?

32
Q

In the Henderson-Hasselbalch equation, if the [A-] is less than [HA] what is the relationship between pH & pKa?

A

pH is less than pKa

33
Q

Define fatty acid

A

A long unbranched chain carboxylic acid containing 10 to 20 carbon atoms.

34
Q

Which blood protein has a sigmoidal O2 binding curve?

A

Hemoglobin

35
Q

Replacing the 6th amino acid of the beta chain of Glu of HbA with Val results in which disease?

A

Sickle Cell Anemia

36
Q

Describe the hydrogen bonding in beta sheets.

A

Between CO & NH on two different polypeptide chains

37
Q

If Fe in hemoglobin is oxidized to 3+, what disease results?

A

Methemoglobin

38
Q

Which amino acid has a pyrrolidine side chain?

39
Q

What are the subunits of Fetal Hemoglobin?

A

a2g2 (alpha2 gamma2)

40
Q

Dehydration of carbonic acid is catalyzed by which enzyme?

A

Carbonic Anhydrase

41
Q

When the acid is exactly half neutralized ([A-] = [HA]), what is the relationship between pH & pKa?

42
Q

The CO2 released from tissues & carried by HbA attaches to which terminal of the polypeptide chain?

A

N-Terminal

43
Q

How many aminoacyl residues are present in loops?

A

More than 4

44
Q

In what disease is Histidine (His F8) replaced by Tyrosine?

A

Hemoglobin M

45
Q

In the Henderson-Hasselbalch equation, if the [A] > [HA], what is the relationship between pH & pKa?

46
Q

What amino acid is responsible for PKU?

A

Phenylalanine

47
Q

In the Henderson-Hasselbalcg equation, if the [A] = [HA], what is the relationship between pH & pKa?

48
Q

Most biomolecules are what?

A

Amphipathic

49
Q

True or False

Amino acids with a non-polar side chain are called hydrophilic.

50
Q

What force is responsible for the stability of aplha-helicies?

A

Hydrogen Bonds

51
Q

An increased concentration in RBCs because of a mutation of hemoglobin results in which disease?

A

Polycythemia

52
Q

The surface of globular proteins contains hydrophilic or hydrophobic groups?

A

Hydrophilic

53
Q

The complete turn of alpha helix contains an average of how many aminoacyl residues?

54
Q

Which blood protein is monomeric?

55
Q

Which blood protein is a good transporter of O2?

A

Hemoglobin

56
Q

How many heme units exist in hemoglobin?

57
Q

What can denature the disulfide bond in peptides?

A

Reducing Agents

58
Q

Salt bridges are comparable in strength to which other intermolecular bond?

A

Hydrogen Bonds

59
Q

Oxidative metabolism produces which gas?

60
Q

How many amino acids make up the alpha chain of hemoglobin?

61
Q

True or False

Solubility of amino acids reflects their ionic character.

62
Q

Which blood protein is a tetrameric structure?

A

Hemoglobin

63
Q

The buffer range or buffer capacity is between what range?

64
Q

What group determines the properties of amino acids?

A

Pendant R Group

65
Q

F8 in myoglobin refers to the ______ Histidine?

66
Q

How many aminoacyl residues join two polypeptide together in a beta bend?

67
Q

The hydrogen bond in the alpha-helix is between which two species?

Biochemistry (17 decks)

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