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1st Term > BIOCHEM PROTEINS > Flashcards

BIOCHEM PROTEINS Flashcards

1
Q

natural product containing nitrogen

A

protein

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2
Q

“proteios”

A

of first importance”

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3
Q

naturally occurring unbranched polymers that contains building blocks of AMINO ACIDS

A

protein

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4
Q

the amino acids in a protein is connected by a?

A

peptide bonds

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5
Q

the structure of a protein is known as

A

native conformation

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6
Q

protein refer to its 3D structure with biological function

A

native conformation

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7
Q

it is the changes in a protein’s native conformation.

A

denaturation

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8
Q

it is a compound containing a carboxyl group and amino group

A

Amino Acids

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9
Q

there are only ___ amino acids found in a human, known as the?

A

20, Standard Amino Acids

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10
Q

Standard Amino Acids are __-amino acids.

A

a-amino acids

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11
Q

a standard amino acid are a-amino acids because they have a?

A

carbonyl group and primary group

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12
Q

the most abundant enantiomer of amino acid?

A

L-amino acid

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13
Q

to represent the D and L enantiomers of the Standard Amino Acids, we use the?

A

Fischer projection

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14
Q

What standard amino acids are found in nature and in proteins?

A

L isomers

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15
Q

a structure with monoamino monocarboxylic acid with non- polar side chain

A

non-polar

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16
Q

it has a hydrophobic chemical characteristics of side chain

A

non-polar

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17
Q

it has a structure of a monoamino monocarboxylic acid with polar side chain

A

neutral polar

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18
Q

it does not ionize at near pH 7 chemical characteristic of a side chain

A

neutral polar

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19
Q

it has a structure of monoamino-dicarboxylic acid

A

acidic polar

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20
Q

it has negative charge near ph7 due to the deprotonation of the carbonxyl group in the side chain chemical characteristic side chain

A

acidic polar

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21
Q

it has a structure of diamino monocarboxylic acid

A

basic polar

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22
Q

it has a postive charge near ph7 due to the protonation of the amino group in the side chain chemical characteristic of side chain

A

basic polar

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23
Q

contains hydrocarbons

A

non-polar amino acid

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24
Q

contains alcohol, phenol, thiol and amide

A

polar-neutral amino acids

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25
Q

contains extra amino group

A

polar basic

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26
Q

donates hydrogen; contains extra carbonyl

A

polar acidic amino acids

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27
Q

standard amino acids that the human body cannot adequately synthesize and must be OBTAINED FROOM DIETARY SOURCES.

A

PVT TIM HALL

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28
Q

only essential for infants normal growth, but becomes nonessential amino acid as they grow into adulthood

A

arginine

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29
Q

contain adequate amounts of these conditionally essential amino acids

A

human milk and infant formula milk

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30
Q

contains all of the essential amino acids in adequate amounts as the body needs.

A

complete dietary protein (high-quality protein)

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31
Q

does not ontin in adequate amounts, relative to the body’s needs

A

incomplete dietary protein

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32
Q

substance that can act as an acid in basic environment and act as a base in an acidic environment

A

amphoteric substance

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33
Q

producing a negatively charged conjugate base known as?

A

carboxylate

34
Q

producing a positively charged conjugate acid known as?

A

quaternarnary ammonium ion

35
Q

the -COOH (carboxyl group) of the standard amino acid is ___ while the -NH2 (amino acid) is __

A

deprotonated or losing; protonated (accepted)

36
Q

a molecule having a positive charge on one side and negative charge on the other

A

zwitterion or dipolar ion

37
Q

a chain of amino acids that is formed when the carboxyl group of the a-carbon of an amino acid reacts with the amino group of the second amino acid.

A

peptide

38
Q

what type of reaction is the formation of peptide?

A

dehydration reaction

39
Q

what is the product after the dehydration reaction?

A

water

40
Q

in a peptide chain, this contains the amino group.

A

n-terminal

41
Q

in a peptide chain, this contains the free carboxyl group

A

c-terminal

42
Q

each hormone is a?

A

nonapeptide

43
Q

pentapeptide neurotransmitters produced by the brain itself

A

enkephalins

44
Q

it is a tripeptide with the sequence Glu-Cys-Gly and serves as an antioxidant

A

glutathione

45
Q

contain ONLY ONE POLYPEPTIDE CHAIN (protein subunit)

A

Monomeric Proteins

46
Q

contain mORE THAN ONE PROTEIN SUBUNITS

A

multimeric proteins

47
Q

only amino acid is present

A

simple proteins

48
Q

contain amino acids and prosthetic groups

A

conjugated proteins

49
Q

denotes the number, kind and sequence of amino acids in protein

A

primary structure

50
Q

a helical (spiral) repeating structure of a polypeptide chain

A

a-helix

51
Q

one turn of the helix comprises ___ amino acid residues

A

3.6

52
Q

the linear distance between corresponding points on successive turns are called

A

pitch

53
Q

a helix breaker

A

proline

54
Q

creates bend in the backbone

A

proline

55
Q

causes crowding which result to steric repulsion

A

presence of bulky groups

56
Q

peptide backbone is almost fully extended

A

b-pleated sheets

57
Q

the over-all three dimensional arrangement of all the atoms in a protein

A

tertiary structure

58
Q

2 types of shapes in tertiary structure of a protein

A

globular sand fibrous shape

59
Q

provides a covalent linkage that binds together the two chains or the two parts of the same chain (2 cysteine far away from each other)

A

disulfide bond

60
Q

this interaction can occur between POLAR NEUTRAL (except cysteine)

A

side-chain hydrogen bonding

61
Q

2 amino residues with ionized side chains. (oppositely charged group)

A

electrostatic attraction (salt bridge)

62
Q

polar groups outward and non-polar groups inward (non-polar groups); weakest interaction.

A

hydrophobic interaction

63
Q

two side chains with the same charge would normally repel each other but they can also be linked via metal ions (2 polar acids with metal in between)

A

meral ion coordination

64
Q

What ate the non polar amino acids?

A

Leucine (Leu, L)
Proline (Pro,P)
Alanine (Ala, A)
Valine (Val, A)
Methionine (Met, M)
Tryptophan (Tyr, W)
Phenylalanine (Phe, F)
Isoleucine (Iso, I)

65
Q

a structure of protein that pertains only to multimeric proteins

A

Quaternary structure

66
Q

The chains may be identical or different. Commonly examples are dimers, trimers, tetramers consisting of two-four polypeptide chains.

A

Quaternary structure

67
Q

Subtle changes in structure at one site on a protein molecule may cause drastic changes in properties

A

Allosteric proteins

68
Q

Means that when one oxygen molecule is bound, it becomes easier for the next molecule to bind.

A

Positive cooperativity

69
Q

The oxygen binding curve of myoglobin

A

Hyperbolic

70
Q

The oxygen binding curve of hemoglobin

A

Sigmoidal

71
Q

Peptides that contain the same kind and number of amino acids but differ in order are called

A

Isomeric peptides

72
Q

disruption of peptide bonds causing liberation of free amino acids

A

Hydrolisis

73
Q

Can be carried out in the presence of strong acids, strong bases and enzymes

A

Hydrolisis

74
Q

causes disruption or unfolding of proteins

A

Denaturation

75
Q

Causes loss of biological activity

A

Denaturation

76
Q

Can be reversible or irreversible

A

Denaturation

77
Q

Results in coagulation and precipitation

A

Denaturation

78
Q

Cleaves hydrogen bonds

A

Heat

79
Q

Can change protein conformation by opening up the hydrophobic regions

A

Detergents or Surface active agents

80
Q

Affects both salt bridges and hydrogen bonds

A

Acids, based and salts

81
Q
  1. Can break disulfide bonds
  2. Latter effect
  3. Make up human hair, contains high percentage of DISULFIDE BONDS
A

Reducing agents, such as 2-mercapoethanol

82
Q

Reverses the preceding reaction, forming nee disulfide bonds, which now hold the molecules together in the desired positins

A

Oxidizing agent

1st Term (15 decks)

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