Proteins Flashcards

1
Q

Linear polymers of amino acids connected by
peptide bonds

A

Proteins

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2
Q

Greek word which means first of importance

A

Proteios

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3
Q

Organic compounds containing an amino group (NH2) and a carboxylic acid group (COOH)

A

Amino acids

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4
Q

The characteristic of having a center attached to four different substituents

A

Chiral

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5
Q

Most common amino acids are a-amino acids. True or false

A

True

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6
Q

All amino acids in the body are L-isomers. True or false

A

True

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7
Q

The only achiral amino acid

A

Glycine

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8
Q

An imino acid and a secondary amine

A

Proline

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9
Q

The characteristic of having an acidic and basic component

A

Amphiprotic

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10
Q

The characteristic of having a positive and negative end

A

Zwitterion

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11
Q

a pH at which amino acids have equal positive and negative charges

A

Isoelectric point

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12
Q

The bond joining amides or an amide bond

A

Peptide bonds

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13
Q

Amino acids that cannot be produced by the body

A

Essential amino acids

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14
Q

The amino acid that is in shortest supply in relation to need or essential amino acids that are present in relatively small amounts and are below the amino acid
requirements

A

Limiting amino acid

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14
Q

Function that provides strength to cells and tissue

A

Structure

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14
Q

Help form the tissues of the hair, nails and outer layer of the skin

A

Keratin

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14
Q

The most abundant protein in the body and used to make connective tissues (bone, skin, muscles, etc.)

A

Collagen

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15
Q

Gives elasticity to tissues

A

Elastin

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16
Q

Function that uses enzymes

A

Catalysis

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17
Q

Speeds up reactions by lowering the activation energy

A

Enzymes

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18
Q

Function that uses muscles

A

Movement

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19
Q

Generates force in a muscle contraction

A

Myosin

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20
Q

Function that delivers substances

21
Q

Carries oxygen from the lungs to the body’s tissues and returns carbon dioxide from the tissues back to the lungs

A

Hemoglobin

22
Chemical messengers released in the bloodstream
Hormones
23
A neurotransmitter also known as the love hormone
Oxytocin
24
Growth hormone
Somatotropin
25
Antidiuretic hormone
Vasopressin
26
Neurohormone that gives feelings of reward
Dopamine
27
Neurohormone produced in the gut. Influences learning, memory, happiness and others
Serotonin
28
The sleep hormone
Melatonin
29
The sleep-wake cycle. Physical, mental, and behavioral changes an organism experiences over a 24-hour cycle
Circadian rhythm
30
Protein from an outside source or some other foreign substance
Antigen
31
The body's own proteins that counteracts foreign proteins
Antibodies
32
The function of proteins to provide a reservoir of an essential nutrient
Storage
33
The function of fighting against outside substances
Protection
34
Its primary function is to supply oxygen to the muscle
Myoglobin
35
Egg white
Ovalbumin
36
A protein complex that stores iron in a soluble, non-toxic form
Ferritin
37
A linear sequence of amino acids and is a small protein that has at least 60 amino acid residues connected by peptide bonds
Primary structure
38
A repetitive conformation of the protein backbone connected by peptide bonds and hydrogen bonds (alpha-helix; beta pleated; random coil)
Secondary structure
39
The complete 3D arrangement of the atoms in a protein
Tertiary structure
40
The spatial relationship and interactions between subunits in a protein that has more than one polypeptide chain
Quaternary structure
41
Composed of amino acids only
Simple proteins or homoproteins
42
Contains a prosthetic group or a non-protein part in addition to protein
Conjugated proteins
43
Proteins derived form simple or conjugated proteins by physical or chemical means
Derived proteins
44
Contains an adequate amount of all the essential amino acids that should be incorporated in the diet
Complete proteins
45
Any protein that lack one or more essential amino acids in correct proportion
Incomplete proteins or partial proteins
46
Compensate for each other's lack of amino acids
Complementary proteins
46
The loss of the secondary, tertiary and quaternary structures of a protein by a chemical or physical agent
Denaturation
47
Cleaves hydrogen bonds
Heat
48
Opens up hydrophobic regions
Detergents
49
Affects salt bridges and H-bonds
Acids and bases, Salts
50
Breaks disulfide bonds
Reducing agents
51
Attacks SH group
Heavy metal ions
52
attacks hydrogen bonds
Alchohol
53
Breaking the peptide bonds by treatment with aqueous acid, base, or certain enzymes
Protein hydrolysis