Chapter 18- Amino acids and proteins Flashcards

1
Q

Secondary structure

A

regular folding patterns seen in localized regions of polypeptide backbone

a and B helix

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2
Q

Tertiary structure

A

Overall shape of protein molecule produced by overall bedding and folding of a protein chain

3

Non covalent interactions and disulfide covalent bonds

A helix and B helix, loops connect

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3
Q

Quaternary structure

A

Overall structure of proteins composed of more than one polypeptide

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4
Q

Enzymes

A

Catalyze biochemical reactions

Ex. Amylase begins digestion of carbohydrates by hydrolysis

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5
Q

Hormones

A

Regulate body functions by carrying messages to receptors

Ex. Insulin facilitates use of glucose for energy generation

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6
Q

Storage proteins

A

Make essential substances available when needed

Ex. Myoglobin stores oxygen in muscles

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7
Q

Transport proteins

A

Carry substances through body fluids

Ex. Serum albumin carries fatty acids in blood
Fatty acids can not easily go through blood because non polar

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8
Q

Structural proteins

A

Provide mechanical shape and support

Example. Collagen provides structure to tendons and cartilage

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9
Q

Protective proteins

A

Defend body against foreign matter

Ex. Immunoglobulin AIDS in destruction of invading bacteria

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10
Q

Contractile proteins

A

Do mechanical work

Ex. Myosin and actin govern muscle movement

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11
Q

Zwitterion

A

Neutral ion with one positive charge and one negative charge

Very soluble

High melting point

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12
Q

Isoelectric point

A

pH at which sample of an amino acid has equal numbers of + and - charges

Net charge= 0

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13
Q

Enantiomers /optical isomers

A

Two mirror -image forms of chiral molecule like alanine

Type of stereoisomers have same formula and atoms with diff connections

Only L in proteins

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14
Q

Primary structure

A

Order

Sequence of amino acids in protein chain connected by peptide bonds

along backbone of protein chain is alternating peptide bonds and a-carbon atoms

DETERMINES PROTEIN SHAPE

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15
Q

Globular protein

A

Water soluble chain is folded in a compact shape with hydrophilic groups

Many are enzymes

Overall shape is tertiary

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16
Q

Fibrous proteins

A

INSOLUBLE

Keratin

Collagen

Elastin

Myosin

Fibrin

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17
Q

Keratin

A

Found in skin, wool, feather, hooves, fingernails

Fibrous

18
Q

Collagens

A

Animal hide, tendons, bone, eye cornea, other CT

Fibrous

19
Q

Elastins

A

Blood vessels, ligaments

Fibrous

20
Q

Myosins

A

Muscle tissue

Fibrous

21
Q

Fibrin

A

Found in blood clots

Fibrous

22
Q

Globular proteins

A

SOLUBLE , hydrophilic groups on outside

insulin

Ribonuclease

Immuglobulins

Hemoglobin

Albumins

23
Q

Insulin

A

Control glucose metabolism

Globular

24
Q

Ribonuclease

A

Enzyme that catalyzes RNA hydrolysis

Globular

25
Immunoglobulins
Involved in immune response Globular
26
Hemoglobin
Oxygen transport Globular
27
Albumins
Perform many transport function in blood; protein in egg white Globular
28
Native protein
Shape in which it functions in living systems
29
Simple protein
Protein composed of only amino acid residues
30
Conjugated protein
Aided by its function by non-amino acid unit Ex. Myoglobin
31
Edmar degradation
Cleaves N-terminal amino acid of polypeptide chain (left)
32
Chemical properties of proteins
Heat Mechanical agitation Detergents Organic compounds pH change Inorganic salts
33
Denaturation
Loss of secondary, tertiary, or quaternary protein structure leaves primary intact Irreversible
34
Functions of proteins
Transport necessary chemicals Support organs or tissues Protect against foreign substances Storage of energy
35
Saponification reaction used to form soaps can be best describe as
Base hydrolysis
36
Soaps
Salts of carboxylic acids Alkali metal salts of long chain carboxylic acids
37
Basic structure of cell membrane consists of
Phospholipid bilayers studded with proteins
38
Lecithin commonly used as
Emulsifying agent
39
Heat affects
Hydrogen bonds and hydrophobic interactions
40
Acids and bases affect
Hydrogen bonds and salt bridges
41
Agitation affects
Hydrogen bonds and hydrophobic interactions
42
Organic compounds are affected by
Hydrophobic interactions