Review Topnotch Flashcards

0
Q

Any substance that resists a change in pH when protons are produced or consumed

A

Buffer

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1
Q

Negative logarithim of hydrogen ion concentration

A

pH

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2
Q

Chemical compound that has a total net charge of zero

A

Zwitterion

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3
Q

pH at which the zwitterion is the predominant form of a chemical comfound

A

Isoelectric pH

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4
Q

Property of water that enables it cleave glycosidic bonds and amide bonds

A

Nucleophile

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5
Q

Property of water that enables it to act as an acid or base

A

Amphoteric

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6
Q

Mkvement of water to a semipermeable membrane

A

Osmosis

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7
Q

Uses carriers

A

Facilitated diffudion

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8
Q

Transport down the concentration agent

A

Passive transport

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9
Q

Uses energy in transport

A

Active transport

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10
Q

Transport an ion along with a molecule

A

Co transport

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11
Q

Bond between two amino acids

A

Peptide ond

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12
Q

Bond between connecting 2 monosacharide forming a disacharide

A

Glycosidic bond

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13
Q

Primary bond of glucosyl residues in glycogen

A

A (1-4) glycosidic bond

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14
Q

Branching bond of glucosyl residues in glycogen

A

A (1-6) glycosidic ond

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15
Q

Bond between nucleotides on DNA strand

A

Phosphodiester bond

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16
Q

Bond between nucleotide base pair

A

Hydrogen bond

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17
Q

Bond between ribose and adenine in adenosine triphosphate

A

B-N glycosidic bond

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18
Q

Between a water molecule and onother polar compound

A

Hydrogen bond

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19
Q

Between two cysteine residues in cystine

A

Disulfide bond

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20
Q

Between glycerol and its fatty acids

A

Ester bond

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21
Q

This equation is used to calculate the concentration of a weak acid and its conjugate base

A

Henderson- hasselbach equation

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22
Q

This equation describes how reaction velocity varies with substrate concentration

A

Michaels- menton equation

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23
Q

This is double reciprocal plot used to calculate Km and Vmax

A

Lineweaver burk

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24
Q

Explain how the free energy generated by the transport of electrons by the ETC is used to produce ATP from ADP+Pi

A

Mitchell chemiosmutic hypothesis

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25
Q

Accepts H+ ions

A

Base

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26
Q

Donates proton

A

Acid

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27
Q

Donates few of its proton

A

Weak acid

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28
Q

Donates almost all of its protons

A

Strong acid

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29
Q

Macromolecules of carbohydrates

A

Glycogen
Sorbitol
Galactidol

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30
Q

Proteins

A

Collagen
Insulin
Hemolobin
Myoglobin

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31
Q

Nucleic acid

A
cAMP
Inosine monophosphate
OMP
cGMP
ADP, ATP
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32
Q

Lipid

A

Palmitate

Vitamin ADEK

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33
Q

State of breaking down complex molecules

A

Catabolism

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34
Q

State of building complex molecules from simpler ones

A

Anabolism

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35
Q

Main currency of enrgy in the body

A

ATP

36
Q

Loss of electrons

A

Oxidation

37
Q

Gain of electrons

A

Reduction

38
Q

Acidic amino acids

A

Aspartate Asp D

Glutmate Glu E

39
Q

Basic amino acids

A

Histidine His H
Arginine Arg R
Lysine Lys K

40
Q

Amino acids with smallest side chain

A

Glycine Gly G

41
Q

Aminomacid with the largest side chain

A

Typtophan Trp W

42
Q

Amino acids which causes collagen kinks

A

Proline Pro P

43
Q

Component of hemoglobin and myoglobin which pays a role in O2 binding

A

Histidine His H

44
Q

Important amino acid that is involve in SAM

A

Methionine Met M

45
Q

Used to diagnose FA deficiency

A

Histidine His H

46
Q

Essential amino acids

A

PVT TIM HALL

Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Arginine
Lysine
Leucine
47
Q

Aminonacid used in haemolobin synthesis

A

Glycine Gly G

48
Q

Precursor of niacin

A

Tryptophan Trp W

49
Q

Precursor of nitric oxide

A

Arginine Arg R

50
Q

Precursor of melanin

A

Tyrosine Tyr Y

51
Q

Precursor of serotonin

A

Trypyophan Trp W

52
Q

Precursor of catecholamines

A

Tyrosine Tyr Y

53
Q

Precursor of melatonin

A

Tryptophan

54
Q

Precursor of GABA

A

Glutamate Glu E

55
Q

Precursor of histamine

A

Histidine His H

56
Q

Precursor of thyroid hormone

A

Tyrosine

57
Q

Precursor of tyrosine

A

Phenylalanine Phe F

58
Q

Precursor of glutathione

A

Glutamate Glu E

59
Q

Beta pleated sheet

A

Secondary

60
Q

Globular or fibrous

A

Tertiary

61
Q

More than one polypeptide is linked together

A

4th

62
Q

Edmans reagent is used to determine this structure

A

Primary

63
Q

Domains

A

Tertiary

64
Q

Hemoglobin most abundant form in adults

A

Hgb A

65
Q

Used to determine levels of glucose by non enzymatic addition of glucose to haemoglobin

A

HBA c

66
Q

Oxidation of the heme component of haemoglobin to Iron which cannot bind oxygen

A

Methemoglobin

67
Q

Form of hemoglobin where CO binds tightly bu reversibly

A

Carboxyhemoglobin

68
Q

Tetrameter consisting of two alpha and gamma chains

A

Fetal hemoglobin

69
Q

Gamma- tetramers in the newborns

A

Hemoglobin barts

70
Q

Basic collagen structure

A

Gly- X-Y

71
Q

X in Gly

A

Proline

72
Q

Y in Gly

A

Hydroxyproline

73
Q

Collagen type

A

Be so totally cool, read books, fetal

 Type 1- bone, skin, tendon
Type 2 - cartilages
Type 3- reticuline
Type 4 - basement membrane
Type 5 - fetal
74
Q

Amount of energy needed for the reaction to go forward

A

Anergy of activation

75
Q

Increase the speed of the reaction by lowering the energy of activation

A

Catalyst

76
Q

Protein catalyst

A

Enzyme

77
Q

Converts one isomers to the other

A

Isomerase

78
Q

Coverts one epimer to the other

A

Epimerase

79
Q

Add carboxyl group to a molecule

A

Carboxylase

80
Q

Catalyze reaction by adding or removing ATP

A

Kinase

81
Q

Removes H+

A

Dehydrogenase

82
Q

Enzymes with different AA compositin but catalayzes the same reaction

A

Isoenzyme

83
Q

Enzyme that requires a cofactor to be active

A

Holoenzyme

84
Q

Protein part of holoenzyme

A

Apoenzyme

85
Q

Vitamin or minerals need by an enzyme to be active

A

Co factor

86
Q

Type of co factor which is permanently complexed with its enzyme

A

Prothatic group

87
Q

Contains another site different from the active site where an effecor binds

A

Allosteric enzyme