Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BIO 024: Biochemistry > Proteins > Flashcards

Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

is an amino acid in which the amino group, the carboxyl group and the hydrogen atom are attached to the a-carbon atom

A

a-amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

All amino acids are alpha-amino acids except _____ which is an imino acid.

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

is an amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain.

A

Nonpolar amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

is an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral.

A

Polar neutral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

is an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain

A

Polar basic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

is an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain

A

Polar acidic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

CLASSIFICATION OF AMINO ACIDS:

G,A,V,L,I,P,F,M,W

A

Nonpolar amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

CLASSIFICATION OF AMINO ACIDS:

S,C,N,T,Q,Y

A

Polar neutral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

CLASSIFICATION OF AMINO ACIDS:

H,K,R

A

Polar basic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

CLASSIFICATION OF AMINO ACIDS:

D,E

A

Polar acidic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

CLASSIFICATION OF AMINO ACIDS:

D,E

A

Polar acidic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

a standard amino acid needed for protein synthesis that must be obtained from dietary sources because the human body cannot synthesize it in adequate amount.

A

ESSENTIAL AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Synthesized by the body.

A

NON-ESSENTIAL AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:

R*,H,M,I,L,K,W,T,F,V

A

ESSENTIAL AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:

C,A,N,D,E,Y,S, Q,G,P

A

NON-ESSENTIAL AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

is a protein that contains all of the essential amino acids in the same relative amounts in which the body needs them. This may or may not contain all of the nonessential amino acids

A

COMPLETE DIETARY PROTEIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

is a protein that does not contain adequate amounts, relative to the body’s needs, of one or more of the essential amino acids

A

INCOMPLETE DIETARY PROTEIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

is an essential amino acid that is missing, or present in inadequate amounts, in an incomplete dietary protein

A

LIMITING AMINO ACID

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

are two or more incomplete dietary proteins that, when combined, provide an adequate amount of all essential amino acids relative to the body’s needs. Ex. Rice and beans servings.

A

COMPLEMENTARY DIETARY PROTEINS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Necessary for the synthesis of neurotransmitter serotonin (5-hydroxytryptamine). A natural relaxant, helps alleviate insomnia by inducing normal sleep; reduces anxiety and depression

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Can be metabolized to niacin Vit. B3 if needed

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Used to synthesized melatonin (5-methoxy-N-acetyltryptamine)

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Precursor of dopamine, norepinephrine, epinephrine
Promotes healthy thyroid functioning

A

Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

enhance energy, increase endurance, and aid in muscle tissue recovery and repair.

A

Valine, Isoleucine, Leucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

lowers elevated blood sugar levels and increases growth hormone production

A

Valine, Isoleucine, Leucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

precursor for L-carathine which is essential for healthy nervous system function.

A

Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

for adequate absorption of calcium and bone development in children

A

Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Is antioxidant. It helps in breakdown of fats and aids in reducing muscle degeneration. Helps lower cholesterol levels by increasing the liver’s production of lecithin; reduces liver fat and protects the kidneys

A

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

principle supplier of sulfur, which inactivates free radicals. Is a natural chelating agent for heavy metals and helps detoxify the body of these metals

A

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Adequate ______ prevents disorders of the hair, skin and nails

A

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Beneficial for healthy nervous system. It may be useful against depression and suppressing appetite

A

Phenylalanine

31
Q

Used to produce dopamine and norepinephrine, chemicals that promote alertness, elevate mood, decrease pain, aid in memory and learning, and reduce hunger and appetite

A

Phenylalanine

32
Q

Type of Phenylalanine:

natural form. May improve rigidity, walking disabilities, speech difficulties and depression associated with Parkinson’s disease

A

D-phenylalanine

33
Q

Type of Phenylalanine:

can be converted into L-tyrosine, which is in turn converted into L-DOPA. L-DOPA is a precursor for dopamine, norepinephrine (noradrenalin), and epinephrine (adrenaline)

A

L-phenylalanine

34
Q

Removes toxic substances released from breakdown of muscle protein during intensive exercise

A

Alanine

35
Q

antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants such as vitamin E and selenium.

A

Cysteine

36
Q

Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.

A

Glutamine

37
Q

Component of skin and is beneficial for wound healing. It acts as neurotransmitter

A

Glycine

38
Q

Important for the synthesis of red and white blood cells.

A

Histidine

39
Q

It is a precursor for histamine which is good for sexual arousal. Improve blood flow.

A

Histidine

40
Q

It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.

A

Threonine

41
Q

Enhances stamina, aids in removal of toxins and ammonia from the body, and beneficial in the synthesis of proteins involved in the immune system.

A

Aspartic Acid

42
Q

plays role in intracellular signaling.

A

Proline

43
Q

plays role in blood vessel relaxation, stimulating and maintaining erection in men, production of ejaculate, and removal of excess ammonia from the body.

A

Arginine

44
Q

Is a molecule that has a positive charge on one atom and a negative charge on another atom, but which has no net charge.

A

Zwitterion

45
Q

It is the pH at which an amino acid exists primarily in its zwitterion form.

A

Isoelectric Point

46
Q

formed by a biochemical reaction that extracts a water(H2O) molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid.

A

Peptide Bonds

47
Q

is a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid

A

Peptide Bonds

48
Q

The linear sequence of amino acids within a protein is considered the _______ of the protein.

A

Primary Structure

49
Q

Proteins are built from a set of only _____ amino acids

A

Twenty (20)

50
Q

The largest group of amino acids have _______ side chains

A

Nonpolar

51
Q

Hydrophobic side chains interact with each other via __________

A

weak van der Waals interactions.

52
Q

TYPES OF PEPTIDE BOND:

w/ 2 or more amino acids

A

Dipeptide

53
Q

TYPES OF PEPTIDE BOND:

w/ 3 or more amino acids joined together in a chain

A

Tripeptide

54
Q

TYPES OF PEPTIDE BOND:

w/ 10 or 20 amino acid residues are present in a chain

A

oligopeptide

55
Q

TYPES OF PEPTIDE BOND:

w/ longer unbranched chain of amino acids

A

Polypeptide

56
Q

Uterus-Contracting Hormone
(also stimulates lactation)

A

Oxytocin

57
Q

Enhances reabsorption of free water and plays a role in Blood pressure control

A

Vasopression (ADH or antidiuretic hormone)

58
Q

pain killers

neuromodulators in the brain and spinal cord; involved with pain perception, movement, mood, behavior, and neuroendocrine regulation

A

Enkephalins

59
Q

Found in most living cells as antioxidant & promote tissue growth

A

Glutathione

60
Q

(governs release of thyrotropin) or TSH or thyroid-stimulating hormone

A

TRH (Thyrotropin Releasing Hormone)

61
Q

Pressor Agent. Can increase blood pressure by vasoconstriction.; can also trigger thirst or the desire for salt. Is responsible for the release of the pituitary gland’s ADH

A

Angiotensin II

62
Q

Inhibits Growth Hormone Release (used to treat ulcers)

A

Somatostatin

63
Q

Hypotensive Vasodilator (acts on smooth muscle)

A

Bradykinin

64
Q

Potent Vasoconstrictor (structurally similar to some
snake venoms)

A

Endothelin

65
Q

Honey Bee Venom (used to treat rheumatism)

A

Mellitin

66
Q

Hyperglycemic Factor (used as an anti-diabetic)

A

Glucagon

67
Q

Pancreatic Hormone (used in treatment of diabetes)

A

Insulin

68
Q

amino acid sequence — drives the folding and intramolecular bonding of the linear amino acid chain, which ultimately determines the protein’s unique three-dimensional shape

A

primary structure

69
Q

Hydrogen bonding between amino groups and carboxyl groups in neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known as alpha helices and beta sheets, these stable folding patterns make up the _____________ of a protein

A

secondary structure

70
Q

The ensemble of formations and folds in a single linear chain of amino acids — sometimes called a polypeptide — constitutes the _______ of a protein.

A

tertiary structure

71
Q

refers to those macromolecules with multiple polypeptide chains or subunits.

A

quaternary structure

72
Q

It is the hydrogen bonding of the peptide hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern.

A

Secondary structure

73
Q

It includes three-dimensional folding pattern or a protein due to side chain interactions

A

Tertiary structure

74
Q

It is the protein consisting of more than one amino acid chain.

A

Quaternary Structure

BIO 024: Biochemistry (16 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions