Structure of Proteins Flashcards

1
Q

Four Types of Structures of proteins

A

– Primary Structure
– Secondary Structure
– Tertiary Structure
– Quaternary

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2
Q

is the order in which amino
acids are linked together in a protein by peptide bonds;

A

Primary Structure

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3
Q

Primary Structure is the order in which amino acids are linked together in a protein by

A

peptide bonds

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4
Q

the backbone of the protein molecule

A

peptide bonds

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5
Q

Every protein has its own unique

A

amino acid
sequence

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6
Q

sequenced and
determined the primary structure for the first
protein - Insulin

A

Frederick Sanger (1953)

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7
Q

primary structure for the first
protein

A

Insulin

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8
Q

The various amino acids present in a protein, whose order is the primary structure of the protein, are linked to each other by

A

peptide linkages

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9
Q

Primary Structure of Proteins have four types of structures which are

A

– Primary Structure
– Secondary Structure
– Tertiary Structure
– Quaternary

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10
Q

The only bond responsible for

the 2o structure of proteins is

A

H- bonding between peptide bonds

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11
Q

one
peptide group and the –N – H of
another peptide linkage farther
along the backbone.

A

–C = O

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12
Q

The two most common types of Secondary Structure of Proteins

A

alpha-helix (α-helix) and
the
beta-pleated sheet (β-pleated sheet).

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13
Q

A single protein chain adopts a shape that
resembles a coiled spring (helix):

A

Alpha-helix (α-helix)

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14
Q

H-bonding between amino acids with in

the same chain –intramolecular H-
bonding

A

Alpha-helix (α-helix)

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15
Q

H-bonding between amino acids with in

the same chain

A

–intramolecular H- bonding

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16
Q

Coiled helical spring

A

Alpha-helix (α-helix)

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17
Q

R-groups stay outside of the helix – not
enough room for them to stay inside

A

Alpha-helix (α-helix)

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18
Q

The helix is so tightly wound that the
space in the center is too small for solvent
molecules to enter

A

Alpha-helix (α-helix)

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19
Q

is so tightly wound that the
space in the center is too small for solvent
molecules to enter

A

helix

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20
Q

Completely extended protein chain
segments in same or different
molecules governed by intermolecular
or intramolecular H-bonding

A

Beta-Pleated Sheets

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21
Q

Completely extended protein chain
segments in same or different
molecules governed by

A

intermolecular or intramolecular H-bonding

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22
Q

H-bonding between different parts of a single chain

A

intramolecular H- bonding

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23
Q

H-bonding between different parts of a
single chain – intramolecular H- bonding

A

Beta-Pleated Sheets

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24
Q

Side chains below or above the axis

A

Beta-Pleated Sheets

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25
has a “U-turn” structure – most frequently encountered
Beta-Pleated Sheets
26
Beta-Pleated Sheets structure that is most frequently enountered
“U-turn” structure
27
Completely extended protein chain segments in same or different molecules
Beta-Pleated Sheets
28
The overall three-dimensional shape of a protein
Tertiary Structure of Proteins
29
Results from the interactions between amino acid side chains (R groups) that are widely separated from each other.
Tertiary Structure of Proteins
30
Defines the biological function of proteins
Tertiary Structure of Proteins
31
Proteins may have, in general, either of the two forms of tertiary structures:
Tertiary Structure of Proteins
32
two forms of tertiary structures:
fibrous globular
33
a covalent, strong, between two cysteine groups; the strongest of the 3o bonds
Disulfide bond:
34
what is the structure of Disulfide bond
Tertiary Structure of Proteins
35
Link chains together and cause chains to twist and bend
Tertiary Structure of Proteins
36
3 Types of Interactions in Tertiary Structure of Proteins
Electrostatic interactions Hydrogen bonding Hydrophobic interactions
37
(ionic interaction, salt linkages):
Electrostatic interactions
38
Salt Bridge between charged side chains of acidic and basic amino acids
Electrostatic interactions
39
Salt Bridge between charged side chains of
acidic and basic amino acids
40
interactions between polar, acidic and/or basic R groups
Hydrogen bonding
41
Occur between non-polar amino acid residues forming non-polar center at the interior of the protein.
Hydrophobic interactions
42
what is the structure of Myoglobin
Tertiary Structure of Proteins
43
An oxygen storage molecule in muscles.
Myoglobin
44
a single peptide chain with one heme unit
Monomer
45
Monomer - single peptide chain with one
heme unit
46
Binds one O2 molecule
Myoglobin
47
Has a higher affinity for oxygen than hemoglobin.
Myoglobin
48
Oxygen stored in -------- molecules serves as a reserve oxygen source for working muscles
myoglobin
49
serves as a reserve oxygen source for working muscles
myoglobin
50
refers to the organization among the various polypeptide chains in a multimeric protein:
Quaternary Structure of Proteins
51
Highest level of protein organization
Quaternary Structure of Proteins
52
Present only in proteins that have 2 or more polypeptide chains (subunits)
Quaternary Structure of Proteins
53
Subunits are generally independent of each other - non covalently bonded
Quaternary Structure of Proteins
54
Subunits are generally independent of each other
non covalently bonded
55
3 kinds of proteins in Quaternary Structure of Proteins
Globular Proteins: Hemoglobin Fibrous Proteins: Alpha-Keratin Fibrous Proteins: Collagen
56
Globular Proteins:
Hemoglobin
57
Fibrous Proteins:
Alpha-Keratin
58
Fibrous Proteins:
Collagen
59
An oxygen carrier molecule in blood
Hemoglobin
60
Transports oxygen from lungs to tissues
Hemoglobin
61
(four polypeptide chains)
Tetramer
62
Tetramer (four polypeptide chains) - each subunit has a
heme group
63
it has a Tetramer (four polypeptide chains) - each subunit has a heme group
Hemoglobin
64
Can transport up to 4 oxygen molecules at time
Hemoglobin
65
Iron atom in heme interacts with oxygen
Hemoglobin
66
atom in heme that interacts with oxygen
Iron
67
Provide protective coating for organs
Fibrous Proteins: Alpha-Keratin
68
Major protein constituent of hair, feather, nails, horns and turtle shells
Alpha-Keratin
69
Mainly made of hydrophobic amino acid residues
Alpha-Keratin
70
Hardness of keratin depends upon
-S-S- bonds
71
More –S-S– bonds make nails and bones
hard
72
More –S-S– bonds make hair
brittle
73
Most abundant proteins in humans
Fibrous Proteins: Collagen
74
(30% of total body protein)
Collagen
75
Major structural material in tendons, ligaments, blood vessels, and skin
Collagen
76
Organic component of bones and teeth
Collagen
77
Predominant structure - triple helix
Collagen
78
Predominant structure of collagen
triple helix
79
Rich in proline (up to 20%) – important to maintain structure
Collagen
80
Collagen is rich in --- up to 20%
proline
81
2 types of fibrous proteins
Alpha-Keratin Collagen