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BIOCHEM LECTURE > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

Proteins came from the Greek word ______ meaning “pre-eminence” or of first importance.

A

PROTEIOS

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2
Q

are chains of amino acids

A

Peptide bond

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3
Q

Proteins are made up of _ _ _ _ ; usually S and traces of Fe, Cu, I, Mn, Zn etc.

A

CHON

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4
Q

these are true proteins found abundantly in both plants and animals.

A

Simple Proteins

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5
Q

soluble in water and dilute neutral salt solutions

A

Albumins

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6
Q

Examples of Albumins

A

serum albumin - blood
lactalbumin - milk
ovalbumin - eggwhite

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7
Q

soluble in neutral dilute salt solutions but NOT in water

A

Globulins

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8
Q

Examples of Globulins

A

ovoglobulin - egg white
edestin - hempseed
myosinogen - muscles
legumin - peas
serum globulin - blood

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9
Q

soluble in dilute acids and alkalis but insoluble in neutral solvents

A

Glutelins

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10
Q

Insoluble in ordinary solvent but soluble in 70% alcohol at about neutral point.
not coagulable by heat.

A

Prolamines

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11
Q

soluble in water, dilute acids and alkalis but not in dilute ammonia
not readily coagulated by heat
strongly basic and occur in tissues in the form of salt combinations with acid substances like heme of the hemoglobin

A

Histones

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12
Q

Examples of Histones

A

globin - hemopglobin
Thymus histone
Scobrone - mackerel

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13
Q

contains small number of amino acids
soluble in water and dilute acids and alkalis
not coagulated by heat

A

Protamines

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14
Q

Example of Protamines

A

Salmin - salmon sperm

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15
Q

soluble in water and neutral solvents

A

Scleroproteins (Albumonoids)

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16
Q

Examples of Scleroproteins

A

Keratin - epidermal tissues
elastin - ligaments
collagen - hides, bones and cartilages

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17
Q

made up of protein molecules combined with non-protein groups

A

Conjugated proteins

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18
Q

Conjugated Proteins

A

Nucleoproteins
Glycoproteins
Phosphoproteins
Chromoproteins
Lipoproteins

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19
Q

Classification of Proteins according to Hydrolysis Products

A

Simple Proteins
Conjugated Proteins
Derived

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20
Q

Simple Proteins

A

Albumins
Globulins
Glutelins
Prolamines
Histones
Protamines
Scleroproteins

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21
Q

combination of histones and protamines with NUCLEIC ACIDS

A

Nucleoproteins

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22
Q

obtained from grandular tissues and germ of grains

A

chromatins

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23
Q

compounds of proteins with a carbohydrate component

A

Glycoproteins

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24
Q

Examples of Glycoproteins

A

mucin - saliva
tendomucoid - tendons
osseomucoid - bones

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25
Q

have the prosthetic group (H3PO4) joined to the protein molecule

A

Phosphoproteins

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26
Q

Examples of Phosphoproteins

A

casein - milk
vitelin - egg yolk

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27
Q

protein compounds with hematin or similar pigments in their molecules

A

Chromoproteins

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28
Q

examples of Chromoproteins

A

cytochromes, hemoglobin, rhodopsin

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29
Q

have fatty substances combined with their molecules like lecithin, cephalin, etc.

A

Lipoproteins

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30
Q

lipoproteins are present in:

A

blood serum, brain tissue, cell nuclei, egg yolk and milk

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31
Q

include substances formed from simple and conjugated proteins

A

Derived

32
Q

2 divisions of derived proteins

A

Primary Protein Derivatives, Secondary Protein Derivatives

33
Q

have undergone slight INTRAmolecular rearrangement through the hydrolytic action of certain physical and chemical agents
synonymous with denatured proteins

A

Primary Protein Derivatives

34
Q

examples of Primary Protein Derivatives

A

Proteans, Metaproteans and Coagulated Proteins

35
Q

insoluble substance resulting from preliminary action of water, dilute acids or enzymes

A

Proteans - myosann, edestan

36
Q

are products of further hydrolysis
soluble in weak acids and alkalies but insoluble in neutral salt soln.

A

Metaproteans - acid metaproteans / alkali metaproteans

37
Q

Insoluble products resulting from either the action of heat, alcohol, UV rays or simple mechanical shaking

A

Coagulated Proteins - cooked

38
Q

products of MORE extensive hydrolysis
mix of fragments of original protein varying in composition and size
NOT coagulated by heat

A

Secondary Protein Derivatives

39
Q

Examples of Secondary PD

A

Primary Proteoses, Secondary Proteoses, Peptones, Peptides

40
Q

are combinations of 2 or more amino acids

A

Peptides

41
Q

According to Biological Significance

A

Transport Proteins - carry/ circulate - hemoglobin (O2), serum albumin(fatty acids)
Storage Proteins - store - Ovalbumin, Ferretin (liver protein)
Protection Proteins - defense - antibodies
Catalytic Proteins - catalyze - enzymes
Structural Proteins - mechanical support - collagen (bones) Keratin (Hair)
Contractile Proteins - nerve impulses - myosin(muscle)
Chemical Proteins - hormones

42
Q

According to conformation/ shape:

A

Fibrous - Collagen, Elastin, Keratin
Globular - Antibodies, Enzymes
Mixed - both

43
Q

are chains of amino acids

A

Peptide bonds

44
Q

two amino molecules can be covalently joined through a substitute linkage termed peptide bond to yield ____?

A

Dipeptide

45
Q

three amino acids can be joined by 2 peptide bonds to form ___?

A

tripeptide

46
Q

4 amino acids can be linked to form a _____?

A

tetrapeptide

47
Q

5 amino acids form ______?

A

pentapeptide

48
Q

few amino acids are joined, the structure is called ____?

A

oligopeptide

49
Q

when many amino acids are joined, the product is called ______?

A

Polypeptide

50
Q

“protein” and “polypeptide” are sometimes used interchangeably, polypeptide generally have molecular weights below 10,000 while PROTEINS have higher molecular weights

A

TRUE

51
Q

The peptide bond is a ________ bond.

A

partial double bond

52
Q

is trans in nature and there is no freedom of rotation because of the partial double bond character

A

C-N bond

53
Q

the angles of rotation that determine the spatial orientation of the peptide chain

A

Ramachandran angles (by Dr GN Ramachandran) / Gopalasamudram Narayanan Ramachandran

54
Q

Properties of Proteins

A

Physical and chemical properties

55
Q

are color less, odorless and tasteless except protein hydrolyzates

A

CHON

56
Q

Proteins are precipitated by:

A

Organic Acids
Inorganic Acids
Salts of Heavy metals
Alkaloidal Reagents
High concentration of neutral salt solution / salting out
Alcohol

57
Q

Levels of organization of CHON:

A

Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure

58
Q

linear arrangement of amino acid in a polypeptide chain joined together by means of peptide linkages (e.g. Insulin)

A

Primary Structure

59
Q

BOTH above, BOTH BELOW, both left, BOTH RIGHT

A

Cis Isomer

60
Q

1 above and 1 below; 1 left and 1 right

A

Trans Isomer

61
Q

Involves the folding of the polypeptide chain.
particularly stable arrangements of amino acid residues giving rise to recurring structural patterns
steric relationship of amino acids

A

Secondary Structure

62
Q

2 types of Secondary Structure

A

Alpha Helix and Beta Pleated Sheet (Pauling & Corey)

63
Q

secondary structure chain formed due to INTRAmolecular H- bonding
has a spiral structure

A

Alpha Helix

64
Q

2 amino acids that disrupt the regularity of the alpha helical backbone conformation

A

Proline & Glycine

65
Q

it means within molecules

A

INTRAMOLECULAR

66
Q

a secondary structure formed due to INTERmolecular H- bonding
are formed by similar hydrogen bonds between continuous sequences of carbonyl and amino groups

A

Beta-Pleated Sheet

67
Q

it means between different peptides

A

INTERMOLECULAR

68
Q

a weak bond due to the weak attraction between a a+H and lone pairs of an atom

A

H-Bond

69
Q

furthermore unfolding of polypeptide chains due to formation of bonds like H-Bond, peptide bond, covalent bond, disulfide bond, ionic bond and hydrophobic interactions

A

Tertiary Structure

70
Q

is the term used to denote a compact globular functional unit of a protein

A

Domain

71
Q

Most complex aspect of protein strand
involves polypeptide chains tightly woven with each other
stabilized by relatively weak interactions
e.g. Hemoglobin

A

Quaternary Structure

72
Q

destruction of the secondary, tertiary and quaternary structures of CHON leading to changes in its physical, chemical and biological characteristics

A

Denaturation of Proteins

73
Q

2 types of Denaturating Agents

A

Physical (heat, UV rays, high pressure)
Chemical (acids & bases,, physical-increased viscosity, Chemical - decreased solubility, Biological - increased digestibility of enzymes)

74
Q

splitting enzyme by acids, bases and protein

A

Hydrolysis

75
Q

Denatured proteins are easily digested in the stomach as compared to undenatured proteins

A

true

BIOCHEM LECTURE (5 decks)

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