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ASS Biochem > Biochem Digging Up Bones > Flashcards

Biochem Digging Up Bones Flashcards

1
Q

DNA TO DNA

A

Replication

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2
Q

DNA TO RNA

A

TRANSCRIPTION

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3
Q

RNA TO PROTEINS

A

Translation

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4
Q

H+ acceptor

A

Base

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5
Q

H+ donor

A

Acid

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6
Q

Donates few of its H+

A

Weak acid

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7
Q

Donates almost almost all of its H+ and forms a weak conjugate

A

Strong acid

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8
Q

A solution that resists changes in its pH when acid or base are added

A

Buffer

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9
Q

The migration of water from the side of a membrane that is hypoosmotic to the side that is hyperosmotic

A

Osmosis

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10
Q

Facilitated transport of a molecule down the concentration gradient by a carrier, does not use energy

A

Passive transport

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11
Q

Facilitated transport of a molecule down the concentration gradient by a carrier, uses energy

A

Active transport

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12
Q

Types of co-transport

A

Symport

Antiport

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13
Q

Process by which matter from the outside an organism is transformed into energy or material for the organism

A

Metabolism

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14
Q

Reactions that break the bonds of complex molecules

A

Catabolism

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15
Q

Reactions which synthesize complex molecules from simpler molecules

A

Anabolism

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16
Q

Energymedium for reqctions inside the cell

A

ATP

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17
Q

Loss of electron

A

Oxidation

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18
Q

Gain of electrons

A

Reduction

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19
Q

Carbohydrate yields # kcal

A

4kcal/gam

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20
Q

Protein yields # kcal

A

4 kcal/gram

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21
Q

Alcohol yields # kcal

A

7kcal/gram

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22
Q

Fats yields # kcal

A

9kcal/gram

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23
Q

Excretory form of protein

A

Urea

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24
Q

Bacteria cqn metabolize urea to ?

A

Ammonia

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25
Q

Where is ethanol is metabolized?

A

Liver

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26
Q

Alcohol inhibits ?

A

Gluconeogenesis

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27
Q

Starch is made in these 2 sites

A

Liver

Muscle

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28
Q

It is the major energy store in the body

A

Fat(triacylglycerol)

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29
Q

2 Sources of monounsaturated fats

A

Olive oil

Canola oil

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30
Q

All plants have unsaturated fats except 2?

A

Coconut oil

Palm oil

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31
Q

Energy source utilized by muscle at rest? Active?

A

At rest: Fat

Active: Carbohydrates

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32
Q

Energy source utilized by brain?

A

Carbohydrates

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33
Q

Number of amino acids in animal metabolism

A

20

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34
Q

ESSENSTIAL AMINO ACIDS

A

phenylalanine, valine, tryptophan, threonine, isoleucine, methionine, Histidine, Argninine, Lysine
[PVT TIM HAL] always trys never tyrs

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35
Q

An amino acid with a sidechain that forms a ring with the amino group of the back bone

A

Proline

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36
Q

These amino acids are hydrophobic and bond together through hydrophobic interactions

A

Valine, Leucine, isoleucine

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37
Q

amino acids with aromatic side chains

A

phenylalanine, tyrosine, tryptophan

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38
Q

amino acids that contain sulfur

A

cysteine, methionine

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39
Q

an imino acid and forms a ring with its own backbone

A

proline

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40
Q

determine the function of the protein

A

side chains

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41
Q

nonpolar side chains, hydrophobic or hydrophilic?

A

hydrophobic

42
Q

Polar acidic amino acids

A

aspartate glutamate

43
Q

polar basic amino acids

A

histidine arginine lysine

44
Q

amino acid that has an imidazole ring, offers buffering at physiologic pH to protein. decarboxylated to histamine

A

histidine

45
Q

2 amino acids that contain hydroxyl groups which can ofrm hydrogen bonds

A

serine and threonine

46
Q

formed by a disulfide bond joining 2 cysteine residues

A

cystine

keratin has many cystine

47
Q

amino acid used in the first step of heme synthesis

A

Glycine

48
Q

blood glycoproteins in diabetics contains glucose linked to this amino acid

A

lysine

49
Q

amino acid with the largest side chain, it is hydrophobic with an aromatic ring

A

tyrosine

50
Q

deficiency of this amino acid can cause hartnup disease and pellagra

A

tryptophan ( coverted to niacin)

51
Q

amino acids that carries nitrogen from the periperal tissues to the liver

A

Alanine glutamine

52
Q

amino acid disrupts the a-helix in a polypeptide

A

proline

53
Q

this amino acid is the phosphorylation site of enzyme modification

A

serine

54
Q

amino acid deaminated to form ammonia

A

glutamine

55
Q

dipolar ions

A

zwitterion

56
Q

essential amino acids

A

(PVT TIM HALL always trys never tyrs)

phenylalanine valine tryptophan threonine isoleucine methionine leucine lysine

57
Q

relatively essential amino acids

A

histidine arginine

58
Q

none essential amino acids

A

(PACT)

proline, arginine(adult) , cysteine, tyrosine

59
Q

disease resulting from adequate inadequate intake of protein, but adequate intake of calories

A

kwashiorkor

60
Q

disease resulting from inadequate intake of both calories and protein

A

marasmus

61
Q

disease presents with unpigmented hair which appears reddish, fatty liver, edema, protruding abdomen

A

kwashiorkor

62
Q

disease presents with retarded growth, emaciation, cachexia, but now low albumin or edema

A

marasmus

63
Q

sequence of amino acids in a polypeptide chain

A

primary structure

64
Q

hydrogen bonding which produces regularly repeated structures( alpha helix and b pleated sheets)

A

secondary structure

65
Q

overall 3 dimensional shape of the protein

A

tertiary structure

66
Q

a number of subunits with spatial arrangement

A

quarternary structure

67
Q

Peptide bonds are formed by joining amino acids by this reaction

A

dehydration

68
Q

Dehydration reaction that forms the peptide bond can be reversed by this reaction

A

hydrolysis

69
Q

all peptide bonds of a polypeptide chain will be broken and the individual amino acids released in this condition

A

strong acid solution at 43°C(110°F) for 24 hours

70
Q

amount of energy which must be added to a reaction to allow it to go forward

A

Gibb’s free energy of activation

71
Q

rate that a reaction occurs

A

reaction velocity

72
Q

increases the speed of a reaction by lowering the reactions energy of activation

A

catalysts

73
Q

protein catalyst which may require a vitamin or mineral cofactor

A

enzyme

74
Q

catalyzes reactions adding or removing nucleoside triphosphate(usally ATP)

A

kinase

75
Q

removes H+

A

dehydrogenase

76
Q

the substance which is recognized by the enzyme and is transformed into the product of the reaction

A

substrate

77
Q

substance formed by the interaction of the substrate and enzyme

A

product

78
Q

part of the enzyme which is catalytic

A

active site

79
Q

attraction between enzyme and substrate

A

affinity

80
Q

theory which states substrate and enzyme always fit each other

A

Lock and key theory

81
Q

theory which states substrates and enzyme fit only at binding

A

induced fit theory

82
Q

enzymes which have different amino acid sequences, but catalyze the same reactions

A

isoenzyme

83
Q

An enzyme which requires a cofactor to be active

A

holoenzyme

84
Q

protein part of a holoenzyme

A

apoenzyme

85
Q

a cofactor which is permanently complexed with its enzyme

A

prosthetic group

86
Q

enzyme which contains another site, different from the active site, at which an effector binds

A

allosteric enyme

87
Q

An enzyme whose substrate is also its effector

A

homotrophic enzyme

88
Q

an enzyme which has a different molecule as an effector

A

heterotrophic enzyme

89
Q

enzyme which may increase or inhibit substrate binding, binding to one site can alter other sites. sigmoidal plot, as opposed to michaelis menten kinetics(hyperbolic)

A

allosteric enzyme

90
Q

activating or inactivating regulatory enzymes

A

phosphorylation
activator- phosphorylase
deactivator- phosphatase

91
Q

Factors that affect the rate of a reaction

A

substrate concentration
temperature
pH

92
Q

Kinetic order: reactions where the rate is independent from substrate concentration

A

zero order

93
Q

Kinetic order: rate is independent from substrate concentration; proportional

A

first order

94
Q

enzymes that have a hyperbolic curve

A

michaelis-menten equation

95
Q

this equation rearranges the michaelis-menten equation so that the line plotted is straight

A

lineweaver-burke plot

96
Q

inhibitor is shaped similar to the substrate and temporarily competes with it for binding sites

A

competitive inhibition

97
Q

binds temporarily to enzyme somewhere other than active site but halts catalysis

A

non-competitive inhibition

98
Q

bind covalently to enzymes and permanently inactivates them

A

irreversible inhibitors

99
Q

catalyze irreversible reactions and are usally the committe step in the pathway

A

allosteric enzyme

100
Q

change in heat of reactants and products

A

enthalpy

101
Q

change in randomness or disorder of the reactants and products

A

entropy

102
Q

reaction occurs spontaneously when change is negative, and not spontaneous when positive

A

free energy

ASS Biochem (1 decks)

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