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BIOCHEM LECTURE > PROTEINS > Flashcards

PROTEINS Flashcards

(75 cards)

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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
have the prosthetic group (H3PO4) joined to the protein molecule
Phosphoproteins
26
Examples of Phosphoproteins
casein - milk vitelin - egg yolk
27
protein compounds with hematin or similar pigments in their molecules
Chromoproteins
28
examples of Chromoproteins
cytochromes, hemoglobin, rhodopsin
29
have fatty substances combined with their molecules like lecithin, cephalin, etc.
Lipoproteins
30
lipoproteins are present in:
blood serum, brain tissue, cell nuclei, egg yolk and milk
31
include substances formed from simple and conjugated proteins
Derived
32
2 divisions of derived proteins
Primary Protein Derivatives, Secondary Protein Derivatives
33
have undergone slight INTRAmolecular rearrangement through the hydrolytic action of certain physical and chemical agents synonymous with denatured proteins
Primary Protein Derivatives
34
examples of Primary Protein Derivatives
Proteans, Metaproteans and Coagulated Proteins
35
insoluble substance resulting from preliminary action of water, dilute acids or enzymes
Proteans - myosann, edestan
36
are products of further hydrolysis soluble in weak acids and alkalies but insoluble in neutral salt soln.
Metaproteans - acid metaproteans / alkali metaproteans
37
Insoluble products resulting from either the action of heat, alcohol, UV rays or simple mechanical shaking
Coagulated Proteins - cooked
38
products of MORE extensive hydrolysis mix of fragments of original protein varying in composition and size NOT coagulated by heat
Secondary Protein Derivatives
39
Examples of Secondary PD
Primary Proteoses, Secondary Proteoses, Peptones, Peptides
40
are combinations of 2 or more amino acids
Peptides
41
According to Biological Significance
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
According to conformation/ shape:
Fibrous - Collagen, Elastin, Keratin Globular - Antibodies, Enzymes Mixed - both
43
are chains of amino acids
Peptide bonds
44
two amino molecules can be covalently joined through a substitute linkage termed peptide bond to yield ____?
Dipeptide
45
three amino acids can be joined by 2 peptide bonds to form ___?
tripeptide
46
4 amino acids can be linked to form a _____?
tetrapeptide
47
5 amino acids form ______?
pentapeptide
48
few amino acids are joined, the structure is called ____?
oligopeptide
49
when many amino acids are joined, the product is called ______?
Polypeptide
50
"protein" and "polypeptide" are sometimes used interchangeably, polypeptide generally have molecular weights below 10,000 while PROTEINS have higher molecular weights
TRUE
51
The peptide bond is a ________ bond.
partial double bond
52
is trans in nature and there is no freedom of rotation because of the partial double bond character
C-N bond
53
the angles of rotation that determine the spatial orientation of the peptide chain
Ramachandran angles (by Dr GN Ramachandran) / Gopalasamudram Narayanan Ramachandran
54
Properties of Proteins
Physical and chemical properties
55
are color less, odorless and tasteless except protein hydrolyzates
CHON
56
Proteins are precipitated by:
Organic Acids Inorganic Acids Salts of Heavy metals Alkaloidal Reagents High concentration of neutral salt solution / salting out Alcohol
57
Levels of organization of CHON:
Primary Structure Secondary Structure Tertiary Structure Quaternary Structure
58
linear arrangement of amino acid in a polypeptide chain joined together by means of peptide linkages (e.g. Insulin)
Primary Structure
59
BOTH above, BOTH BELOW, both left, BOTH RIGHT
Cis Isomer
60
1 above and 1 below; 1 left and 1 right
Trans Isomer
61
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
Secondary Structure
62
2 types of Secondary Structure
Alpha Helix and Beta Pleated Sheet (Pauling & Corey)
63
secondary structure chain formed due to INTRAmolecular H- bonding has a spiral structure
Alpha Helix
64
2 amino acids that disrupt the regularity of the alpha helical backbone conformation
Proline & Glycine
65
it means within molecules
INTRAMOLECULAR
66
a secondary structure formed due to INTERmolecular H- bonding are formed by similar hydrogen bonds between continuous sequences of carbonyl and amino groups
Beta-Pleated Sheet
67
it means between different peptides
INTERMOLECULAR
68
a weak bond due to the weak attraction between a a+H and lone pairs of an atom
H-Bond
69
furthermore unfolding of polypeptide chains due to formation of bonds like H-Bond, peptide bond, covalent bond, disulfide bond, ionic bond and hydrophobic interactions
Tertiary Structure
70
is the term used to denote a compact globular functional unit of a protein
Domain
71
Most complex aspect of protein strand involves polypeptide chains tightly woven with each other stabilized by relatively weak interactions e.g. Hemoglobin
Quaternary Structure
72
destruction of the secondary, tertiary and quaternary structures of CHON leading to changes in its physical, chemical and biological characteristics
Denaturation of Proteins
73
2 types of Denaturating Agents
Physical (heat, UV rays, high pressure) Chemical (acids & bases,, physical-increased viscosity, Chemical - decreased solubility, Biological - increased digestibility of enzymes)
74
splitting enzyme by acids, bases and protein
Hydrolysis
75
Denatured proteins are easily digested in the stomach as compared to undenatured proteins
true

BIOCHEM LECTURE (5 decks)

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