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[2ND YEAR] CCP 4 - Pharmaceutical Biochemistry (Lec) > PRELIM 02 - Proteins > Flashcards

PRELIM 02 - Proteins Flashcards

1
Q

Are polymers of amino acids

A

Proteins

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2
Q

Are molecules that contains an amino, carboxyl, and side chain group

A

Amino acid

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3
Q

A chemical group that gives identity to the amino acid

A

Side chain group (R)

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4
Q

All amino acids, except __________ have at least one stereocenter and are achiral

A

Glycine

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5
Q

Molecules that contain both positive and negative charges

A

Zwitterion

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6
Q

Proton donor

A

Bronsted acid

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7
Q

Proton acceptor

A

Bronsted base

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8
Q

The pH at which the net charge of an amino acid/peptide is zero

A

Isoelectric pH (pl)

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9
Q

Is an amide bond between the α-carboxyl group of one amino acid and the α-amino group of another amino acid

A

Peptide bond

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10
Q

Molecules that are two or more amino acids linked by peptide bonds

A

Peptides

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11
Q

Are amino acids not or inadequately synthesized by the body; essential in the diet

A

Essential amino acids

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12
Q

Are amino acids that can be synthesized in the body; not required in the diet

A

Non-essential amino acids

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13
Q

Refers to the spatial arrangement of atoms in a protein

A

Conformation

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14
Q

The three-dimensional structure of a protein is called __________

A

Native conformation

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15
Q

Are proteins in any of their functional, folded conformation

A

Native proteins

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16
Q

4 levels of protein organization

A

Primary, Secondary, Tertiary, Quaternary

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17
Q

It refers to the sequence of amino acids in a polypeptide chain (Levels of protein organization)

A

Primary structure

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18
Q

It refers to the ordered 3D arrangements in localized regions of a polypeptide chain (Levels of protein organization)

A

Secondary structure

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19
Q

3 types of secondary structure of proteins

A

α-Helix, β-sheet, Random coil

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20
Q

Spiral structure; stabilized by intramolecular hydrogen bonds (Types of secondary structure of proteins)

A

α-Helix

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21
Q

Pitch of α-Helix

A

5.4 Angstrom

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22
Q

It is formed when 2 or more polypeptides line up side by side (Types of secondary structures of proteins)

A

β-sheet/β-pleated sheet

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23
Q

2 types of β-sheets/β-pleated sheets

A

Anti-parallel β-sheet, Parallel β-sheet

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24
Q

These are non-repetitive structures; an irregular or unique conformation (Types of secondary structures of proteins)

A

Random coils

25
Q

Are structures that are combinations of α and β-strands

A

Supersecondary structures

26
Q

4 examples of supersecondary structures

A

βαβ unit, αα unit, β-meander, Greek key

27
Q

It refers to the three-dimensional conformation of the entire polypeptide (Levels of protein organization)

A

Tertiary structure

28
Q

Are proteins composed of a polypeptide chain arranged in long strands or sheets

A

Fibrous proteins

29
Q

2 examples of fibrous proteins

A

Collagen, Keratin

30
Q

Are proteins composed of a polypeptide chain folded into compact, spherical structure

A

Globular proteins

31
Q

2 examples of globular proteins

A

Enzymes, Hemoglobin

32
Q

It refers to the spatial arrangement of polypeptide subunits (Levels of protein organization)

A

Quaternary structure

33
Q

Quaternary structure with 2 subunits

34
Q

Quaternary structure with 3 subunits

35
Q

Quaternary structure with 4 subunits

36
Q

2 examples of glucose homeostatic proteins; they control carbohydrate metabolism by binding on specific receptors

A

Insulin, Glucagon

37
Q

Insulin and glucagon are synthesized at the __________

38
Q

Insulin is synthesized at __________

39
Q

Glucagon is synthesized at __________

40
Q

Hormone of nutrient abundance; a protein hormone consisting of two amino acid chains linked by disulfide bonds

41
Q

3 major targets for insulin

A

Liver, Skeletal muscle, Adipose tissue

42
Q

A 29-amino acid polypeptide hormone that is a potent hyperglycemic agent

43
Q

Refers to the breakdown of glycogen to glucose

A

Glycogenolysis

44
Q

Refers to the synthesis of glucose from lactic acid and non-carbohydrates

A

Gluconeogenesis

45
Q

2 examples of hemeproteins

A

Hemoglobin, Myoglobin

46
Q

Hemoglobin’s major role is __________

A

Oxygen transport

47
Q

Myoglobin’s major role is __________

A

Oxygen storage

48
Q

Tetramer of hemoglobin

49
Q

Other name for immunoglobulin; is a y-shaped molecule produced by B-cells during adaptive immune response

A

Antibodies

50
Q

Immunoglobulin is composed of __________ subunits; __________ heavy chains and __________ light chains

A

4 subunits, 2 heavy chains, 2 light chains

51
Q

Immunoglobulin is composed of: __________, __________, and __________

A

Constant regions, Variable regions, Hinge

52
Q

5 antibody isotypes

A

IgM, IgA, IgD, IgG, IgE

53
Q

The antibody which serves as protection for primary infections

54
Q

The antibody that is commonly found in human secretions like tears, mucous, and saliva

55
Q

The cell attached antibody which function is still under study

56
Q

The most dominant antibody in humans; this antibody is responsible for secondary immune response

57
Q

The antibody responsible for allergic reactions

58
Q

It refers to the disruption of the protein conformation as well as its function

A

Denaturation

[2ND YEAR] CCP 4 - Pharmaceutical Biochemistry (Lec) (19 decks)

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