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Biochemistry Lecture > Proteins > Flashcards

Proteins Flashcards

1
Q

Made up of amino acids that are joined together by ___

A

Peptide bonds

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2
Q

There are __ naturally occurring amino acids

A

20

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3
Q

Most genetic information directs the synthesis of protein

A

Central Dogma

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4
Q

__ properties of amino acids that play an important role in their ___

A

Chemical , Function

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5
Q

8 Functions of Proteins

A 
Structure
Catalysts
Movement
Transport
Hormones
Protection
Storage 
Regulation
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6
Q

Protein function that is constituent of the skin, bone and hair

A

Structure – Keratin and collagen

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7
Q

2 properties of collagen and keratin that is attributed to their role

A

Fibrous – Hydrophobic

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8
Q

Protein function that hastens all reactions in the living system

A

Catalyst

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9
Q

Protein that hastens all metabolic reactions

A

Enzymes

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10
Q

Example of roles of enzyme in the body

A

Conversion of Alcohol by alcohol dehydrogenase
Digestion of carbs by salivary amylase
For blood clotting
Muscle contraction

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11
Q

Protein Function governed by muscle proteins

A

Movement – Myosibn and Actin filaments

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12
Q

Protein function chiefly done by hemoglobin

A

Transport

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13
Q

Protein function done by fibrinogen and antibodies

A

protection

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14
Q

Protein function with examples of insulin, oxytocin, and human growth hormone

A

Hormones

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15
Q

Protein function with examples of Casein, ovalbumin and ferritin

A

Storage

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16
Q

Protein function storage (Analogy)
Casein : ___
Ovalbumin : ____
Ferritin : ____

A

Casein : milk
Ovalbumin : eggs and nutrients of newborn
Ferritin : Iron

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17
Q

Protein Function that controls when the expression of genes should take place

A

Regulation

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18
Q

2 Types of proteins

A

Globular and Fibrous proteins

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19
Q

Predominant type of protein

A

Globular protein

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20
Q

type of protein for structural purposes

A

fibrous protein

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21
Q

type of protein that have a characteristic of elongated wires

A

Fibrous proteins

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22
Q

type of protein that is insoluble in water and have high percentage of secondary structure – alpha helix and beta pleated sheets

A

Fibrous protein

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23
Q

Type of protein that is the vast majority of all known enzymes

A

Globular protein

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24
Q

Predominant type of protein

A

globular protein

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25
Q

Type of protein that forms colloid with water

A

globular protein

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26
Q

type of of protein that is spherical in shape

A

globular protein

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27
Q

Building blocks /monomer unit of protein

A

amino acid

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28
Q

Compound that contains both the amino group and carboxyl group

A

amino acid

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29
Q

An amino acid in which the amino group is on the carbon adjacent to the carboxyl group

A

Alpha amino acid

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30
Q

Alpha amino acids are commonly written in their ___ form

A

unionized form

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31
Q

Amino acids’ internal salt form

A

zwitterion

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32
Q

a form of an amino acid with the presence of charged group (positive - amino group ; negative - carboxyl group)

A

zwitterion

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33
Q

form of an amino acid that results to net charge of 0

A

zwitterion

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34
Q

All amino acids have at least one stereocenter and are chiral except for

A

Glycine (Gly, G)

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35
Q

Vast majority of amino acids have this kind of configuration

A

L-configuration

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36
Q

2 types of configuration at the alpha carbon

A

L-configuration

D-configuration

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37
Q

Examples of D-configuration proteins

A

sugars and carbs

38
Q

type of configuration that is prevalent in nature

A

L-configuration

39
Q

Amino acids that are nonpolar (hydrophobic)

A 
Alanine (Ala, A)
Glycine (Gly, G)
Valine (Val, V)
Isoleucine (Ile, I)
Leucine (Leu, L)
Methionine (Met, M)
Phenylalanine (Phe, F)
Proline (Pro, P)
Tryptophan (Trp, W)
40
Q

Alanine (Ala , A) Side chain

A

Aliphatic (Hydrocarbon) side chain

41
Q

Glycine (Gly, G) side chain

A

No stereocenter ; not chiral

42
Q

Valine (Val, V) side chain

A

Aliphatic (hydrocarbon) side chain

43
Q

Isoleucine (Ile, I) side chain

A

Aliphatic (hydrocarbon) side chain

isomer of isoleucine

44
Q

Leucine (Leu, L) side chain

A

Aliphatic (hydrocarbon) side chain

45
Q

Methionine (Met, M) side chain

A

Aliphatic (hydrocarbon) side chain

Additional Sulfur

46
Q

Phenylalanine (Phe, F) side chain

A

Aromatic Ring side chain

47
Q

Proline (Pro, P) side chain

A

Imino acid becaue of Secondary amino group

48
Q

Tryptophan (Trp, W) side chain

A

Indole Ring (2 aromatic rings)

49
Q

Amino acids with Polar and neutral / uncharged side chains

A 
Asparagine (Asn, N)
Glutamine (Gln, Q)
Tyrosine (Tyr, T)
Threonine (Thr, R)
Serine (Ser, S)
Cysteine (Cys, C)
50
Q

Asparagine (Asn, N) side chain

A

aliphatic hydrocarbon and amide side chain

51
Q

Glutamine (Gln, Q) side chain

A

aliphatic hydrocarbon and amide side chain

52
Q

Tyrosine (Tyr, Y) side chain

A

aromatic ring and hydroxyl group side chain

53
Q

Threonine (Thr, R)

A

Aliphatic hydrocarbon and hydroxyl group side chain

54
Q

Serine (Ser, S) side chain

A

Aliphatic hydrocarbon and hydroxyl group side chain

55
Q

Cysteine (Cys, C)

A

Aliphatic hydrocarbon and thiol / sulfihydryl group side chain)

56
Q

Amino acids with acidic and charged side chains

A 
Aspartic Acid (Asp, D)
Glutamic acid (Glu, E)
57
Q

Aspartic acid (asp, D) side chain

A

Aliphatic hydrocarbon and additional carboxyl group side chain

58
Q

Glutamic acid (Glu, E) side chain

A

Aliphatic hydrocarbon and additional carboxyl group side chain

59
Q

Amino acids with basic and charged side chains

A

Arginine (Arg, R)
Histidine (His, H)
Lysine (Lys, K)

60
Q

Arginine (Arg, R) side chain

A

Aliphatic hydrocarbon and guanidino with additional amino group side chain

61
Q

Histidine (His, H) side chain

A

Aliphatic hydrocarbon and aromatic ring and additional amino group

62
Q

Lysine (Lys, K) side chain

A

Aliphatic hydrocarbon and additional amino group

63
Q

Ability to rotate on its plane

A

Chirality of the Carbon

64
Q

If we add a strong base such as NaOH to the solution and bring its pH to 14

A

a proton is transferred FROM the NH3+ making it a negative ion

65
Q

If we add a strong acid such as HCl to bring the pH of the solution to 0.0

A

it denotes a proton TO the COO- making it a Positive Ion

66
Q

The pH at which majority of the molecules of a compound in a solution has no net charge

A

Isoelectric point

67
Q

Isoelectric point has how many charge

A

0

68
Q

Formula of Isoelectric point (pI)

A

(Pk1+Pk2) / 2

69
Q

Amino acid that is easily oxidized

A

Cyteine convertine -SH group to S-S disulfide

From Cysteine to Cystine

70
Q

Amino acids that are used in protein of BRAIN TRANSMITTERS

A

Phenylalanine, Tryptophan, Tyrosine

71
Q

Amino acids that undergo Hydroxylation (oxidation)

A

Proline - hydroxyproline
Lysine - hydroxylysine
Cysteine - cystine

72
Q

Amino acids that undergo Iodination

A

Tyrosine - Thyroxine

73
Q

AMIDE BOND between the alpha carboxyl group of an amino acid and amino group of another amino acid

A

Peptide bond

74
Q

At physiological pH (7.4) the carboxyl group is ____, the amino group is ____ so an isolated amino acid would bear both a positive and negative charge

A

carboxyl group - Unprotonated

amino group - protonated

75
Q

the different structure and function of amino acids are attributed by its

A

R-group

76
Q

A short polymer of amino acids joined by peptide bonds; they are classified by the number of amino acids in the chain

A

peptide

77
Q

a molecule containing two amino acids joined by a peptide bond

A

Dipeptide

78
Q

a molecule containing three amino acids joined by peptide bonds

A

Tripeptide

79
Q

a macromolecule containing many amino acids joined by peptide bonds

A

Polypeptide

80
Q

a biological macromolecule containing at least 30-50 AMINO ACIDS joined by peptide bonds

A

Protein

81
Q

individual amino acid units are referred to as

A

Residues

82
Q

Formula of number of amino acid residues

A

number of amino acids - 1

83
Q

A peptide bond is typically written as

A

carbonyl group bonded to an N-H group

84
Q

There is about __% double bond character to the C-N bond of a peptide bond

A

40%

85
Q

Peptide bond between two amino acid shows what kind of structure

A

PLANAR

86
Q

the amino acid at the end of the chain having the free -COO- group

A

C-terminal amino acid

87
Q

the amino acid at the end of the chain having the free -NH3+ group

A

N-terminal amino acid

88
Q

At a pH above (more basic than) its pI it has a net charge of

A

NEGATIVE NET CHARGE

89
Q

At a pH below (more acidic than) its pI it has a net charge of

A

POSITIVE NET CHARGE

90
Q

Proteins are ____ in water at their isoelectric points
A. More soluble
B. Least soluble

A

B. Least soluble / Insoluble

91
Q

Proteins at their isoelectric points can be __ from solution

A

precipitated meaning it can easily be separated since they are insoluble at this point

92
Q

Amino acids are ___ and they can exist as ___

A

Stereoisomers ; Enantiomer

Biochemistry Lecture (8 decks)

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