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Bichem > quiz one essentials > Flashcards

quiz one essentials Flashcards

1
Q

Fatty acid composition

A

long hydrocarbon chains with terminal carboxylic acids

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2
Q

Amino acid composition

A

amino and carboxylate groups

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3
Q

triglycerol composition

A

3 fatty acid chains liked to glycerol by ester bonds

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4
Q

Protein composition

A

amino acid liked via amide peptide bond

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5
Q

Ester composition

A

acid and alcohol

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6
Q

Name the 3 ketone bodies

A

Acetoacetate, acetone(volatile), 3-hydroxybutyrate

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7
Q

Name body composition in regards to macromolecules

A 
water
protein
lipids
calcium phosphate 
carbohydrates
nucleic acids
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8
Q

draw functional groups

A

do it

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9
Q

compare glucose and fructose

A

glucose has 6 membered ring and fructose has 5 membered ring. glucose has 1 CH2OH and fructose has 2 CH2OH. glucose is alcohols and aldehyde and fructose is alcohols and ketone

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10
Q

ATP

A

2 phosphoanhydride
1 phosphomonoester
1 glycosidic bond
2 alcohol groups

ADP is same but only one phosphoanhydride bond

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11
Q

glycerol

A

3 OH groups on carbon chain

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12
Q

Pyruvate and lactate

A

pyruvate (has alpha ketone)

lactate(has alpha hydroxy group)

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13
Q

What atoms have high electron affinity?

A

N,O,S

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14
Q

Polar and non polar

A

polar bonds are covalent bonds between atoms with different electronegativity and result in the electron with a high electron affinity having a partial negative charge

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15
Q

Water and polarity things

A
  • H atoms in water assume a partial positive charge and O atoms assume the partial negative charge.
  • the partial charges allow water molecules to be attracted ta each other via hydrogen bonds
  • also allow for hydrogen bonds to form with water and other electronegative atoms
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16
Q

hydrophillic molecules

A
  • charged based interactions is required for water solubility.
  • the material must be charged or have polar bonds that can associate with charges of water
  • like dissolves like because charged interacts with charged.
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17
Q

hydrophobic molecules

A
  • molecules with no charge (non polar)
  • cannot interact with charges of water
  • are soluble in fats because like dissolves like
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18
Q

solubility rule of thumb

A

C:N+O ratio
if ratio is less than 7:1, the molecule should be soluble in water. (higher partial charge)
-how would you make a molecule more soluble? Add NOS

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19
Q

Amphipathic molecules

A

molecules with distinct hydrophobic and hydrophilic regions

  • fatty acid chain
  • make micelles and bi layers
  • micelles transfer hydrophobic lipids within blood(monolayer vesicles with hydrophilic heads on outide)
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20
Q

Phosphate transfer reaction

A

a phosphate group is transferred to another molecule(usually a hydroxyl group of glucose)

  • forms a phosphomonoester bond
  • enzyme used to phosphorylate is kinase(P has to come from ATP)
  • fasting=phosphorylated
  • well-fed=dephosphorylated
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21
Q

Phosphate cleavage reaction

A

phosphate is removed from a compound

  • enzyme used to dephosphorylate is phosphatase
  • bond is hydrolyzed to inorganic phosphate
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22
Q

rearrangement reactions

A

bonding pattern within a compound undergoes rearrangement but the overall molecule formula is the same

  • structural isomers
  • help make it fit for an enzyme
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23
Q

Condensation reactions

A

condensation of two molecules to form one molecule

  • biproduct is water
  • requires energy
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24
Q

Hydrolysis reactions

A

disassembly of polymers to their monomeric units

-requires water, not energy

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25
Q

Oxidation reactions

A

Loss of hydrogen atoms/ gain of oxygen atoms

  • dehydrogense is enzyme that removes 2 hydrogens
  • oxidase is enzyme that adds 1 oxygen
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26
Q

Reduction reactions

A

Gain of hydrogen atoms/ loss of oxygen atoms

-reductase is addition of 2 hydrogen atoms

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27
Q

Acid/ Base reactions

A
  1. most biochemical reactions occur in water
  2. acid releases proton and base accepts proton
  3. strong acids completely dissociate in water (no pka)
  4. weak acids partially dissociate (have pka)(how much they dissociate depends on the environment
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28
Q

pH and hydrogen concentration

A

more acid means lower pH which means more H concentration

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29
Q

Strong/Weak acids

A

strong acids completely dissociate (no pKa)

weak acids patially dissociate (pKa)

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30
Q

Ka/pKa

A

Ka defines the extent of dissociation of a weak acid.

  • Ka is converted to pKa to avoid small numbers
  • lower the pKa, the stronger the acid
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31
Q

pKa range fro carboxylic acids and ammonium ions

A

pKa for carboxyllic acid: 2-7
pKa from ammonium ion: 6-11
(when they are deprotonated)

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32
Q

Carboxyllic acid deprotonation

A

unchargerd (RCOOH) to charged (RCOO-)

-uncharged acidic form

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33
Q

Ammonium ion deprotonation

A

charged (RNH3+) to uncharged (RNH2)

-charged acidic form

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34
Q

concentration trends of conjugate bases and weak acids according to pKa and pH

A
  • when pH=pKa, conjugate base=weak acid concentration
  • when pH>pKa, conjugate base>acid concentration
  • when pH
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35
Q

Henderson-Hasselbach equation

A

pH=pKa+log(conjugate base)/(acid)

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36
Q

When is a drug absorbed

A

uncharged form is absorbed

-charged from is not absorbed

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37
Q

name the 2 factors that determine buffer effectiveness

A
  1. the buffers pH range

2. the buffers concentration (buffering capacity)

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38
Q

pH range of a buffer

A

+/- one pH unit from the pKa of the weak acid

-pKa is 4, effective range is 3 and 5 is effective pH range

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39
Q

Addition of acid/ base to buffer

A
  • when acid is added, the excess protons will bind to conjugate bases
  • when base is added, weak acid will deprotonate to allow H+ to bind to excess bases.
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40
Q

G-protein coupled receptor

A
  • extracellular ligand binding domain
  • seven transmembrane spanning domain(helices)
  • G-protein activation domain
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41
Q

G-protein

A
  • heteromeric (large)

- Beta, gamma, and alpha subunits

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42
Q

Beta and gamma G-protein subunits

A

-act as membrane localized docking site for inactve alpha subunit

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43
Q

alpha subunit of G-protein

A

-binds guanosine nucleotides (GTP and GDP)
-has inherent ability to hydrolyze GTP to GDP
-GTP activates
-GDP turns off
Gs-stimulates and Gi-inhibits
-interacts with adenylyl cyclase
Gq interacts with phospholipase C

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44
Q

Adenylyl cyclase

A
  • integral membrane enzyme
  • activated by Galpha protein
  • hydrolyzes ATP to get cAMP
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45
Q

cAMP

A
  • cyclic adenosine monophosphate
  • second messenger for intercellular signalling
  • interacts with protein kinase A
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46
Q

Protein Kinase A

A
  • enzyme made of 2 regulatory subunits and 2 catalytic subunits
  • regulatory subunits interact with cAMP and release catalytic subunits
  • cAMP dependent
47
Q

Protein Kinase A catalytic subunits

A
  • phosphorylate target proteins and enzymes

- make them function as intracellular effectors drivin by extracellular signals

48
Q

intracellular effectors

A
  • ion channels: regulate the flow of specific ions across membrane
  • enzymes: regulate metabolic pathways
  • DNA-binding proteins: regulate gene expression
  • PHOSPHORYLATION CAN TURN ON OUR OFF
49
Q

Protein phosphatase

A
  • enzymes
  • hydrolytically cleave phosphate esters
  • dephosphorylate effector proteins that were phosphorylated by protein kinase A
50
Q

cAMP phosphodiesterase

A
  • enzyme

- converts cAMP to 5’AMP which is not a signaling protein

51
Q

Vibrio Cholera

A
  • continuous permanent activation of adenylyl cyclase.
  • ARF A1 catalyzes ADP ribosylation of Gs and prevents it from hydrolyzing GTP-GDP and deavtivating adenylyl cyclase
  • colon reabsorption is overwhelmed so you have permanent diarrhea/ dehydration
52
Q

Gq protein

A
  • hormone (epinephrine) receptor activated

- interacts with phospholipase C

53
Q

Phospholipase C

A
  • membrane localized
  • cleaves lipid bi-layer
  • PIP2 to IP3 and DAG
54
Q

PIP2

A
  • phosphatidylinositol 4,5-bisphosphate

- membrane phospholipid

55
Q

IP3

A
  • Inositol 1,4,5-triphosphate
  • binds to ER receptor
  • activates Ca2+ channels
  • releases Ca2+ into cytosol
56
Q

DAG

A
  • Diacylglycerol
  • remains in the membrane
  • activates protein kinase C
57
Q

Protein Kinase C

A
  • cAMP independent
  • phosphorylates proteins
  • activated by Ca2+ and DAG
58
Q

Ligands that stimulate IP3 and DAG signaling

A
  • neurotransmitters
  • hormones
  • growth factors
59
Q

Calcium signaling

A
  • Activation of glycogen degradation in liver in response to epinephrine binding the adrenergic receptors
  • 4Ca2+ bind to calmodulin
  • calmodulin-Ca complex conformational change
  • complex can activate enzymes involved in metabolism
  • Ca2+ can act as a secondary messenger
60
Q

Insulin

A
  • protein hormone (water soluble)
  • produced in beta cells of islets in pancreas
  • stored in secretory granules
  • anabolic effector (promotes production of glycogen, tricyglycerols, and protein)
  • stored in adipose tissue and muscle
61
Q

Glucagon

A
  • protein hormone (water soluble)
  • produced in alpha cells of islets in pancreas
  • catabolic effector(production of glucose from the liver)
  • maintains blood glucose levels by activation of gluconeogenesis and glycogenolysis
62
Q

Glucose stimulation of insulin

A
  • increase in blood glucose results in increase of insulin release
  • beta cells produce more insulin
63
Q

Amino acid stimulation of insulin

A
  • ingesting protein results in increased concentrations of amino acids
  • increased levels of insulin released (to promote uptake of amino acids to muscles)
  • glucagon is also released to compensate
64
Q

gastrointestinal stimulation of insulin

A

-peptide hormones are released from small intestine as anticipatory insulin release stimulators in response to food intake

65
Q

Factors that negatively affect insulin secretion

A
  • scarcity of dietary fuels

- increase in epinephrine levels

66
Q

Epinephrine

A
  • secreted by adrenal medulla
  • triggered by stress, trauma, exercise
  • mobilizes glucose from liver and fatty acid from adipose tissue
  • can override normal glucose-stimulated release of insulin
67
Q

Insulin binding

A
  • binds and activates tyrosine kinase
  • phosphorylates insulin receptor substrates (IRS-IRSp)
  • now phosphorylated active proteins that effect gene expression, cell metabolism, and cell growth
68
Q

Gluc4

A
  • insulin sensitive glucose transporter

- primarily found in muscle and adipose tissue

69
Q

mechanism of glucose transporter

A
  1. glucose transporters move from cell membrane to intracellular storage pool
  2. vesicles fuse to form endosome
70
Q

How long does it take to transport glucose into muscle and adipose tissue?

A

seconds

71
Q

How long does it take for insulin induced changes in enzymatic activity to occur?

A

minutes-hours

72
Q

How long does it take for production of enzymes in response to insulin?

A

hours-days

73
Q

Insulin sensitive

A

skeletal muscle and adipose tissue

74
Q

Insulin insensitive

A

active transport: epithelia of intestine, renal tubes, choroid plexus
facilitated transport: lens of cornea, liver, brain, leukocytes

75
Q

Gycogenesis

A
  • insulin receptor on

- glucose-glycogen

76
Q

Gycogenolysis

A
  • glucagon and epinephrine on

- glycogen-glucose

77
Q

Gluconeogenesis

A
  • glucagon and epinephrine on

- non carbohydrate source-glucose

78
Q

glucagon secretion stimulus

A
  • increased amino acids

- increased epinephrine levels

79
Q

glucagon signaling

A

SAME AS CAMP SIGNALING

80
Q

effects of glucagon signaling

A
  • rise in blood glucose
  • activates lipolysis in adipose
  • amino acid uptake in liver
81
Q

ketogenesis

A
  • break down of amino acids to form ketone bodies

- glucagon and epinephrine up

82
Q

lipolysis

A
  • break down of fats to make fatty acids

- glucagon and epinephrine up

83
Q

Amino Acid structure

A
  • carbon atom, amino group, carboxylic acid, single hydrogen

- R group gives distinction

84
Q

Polar amino acids

A

-acidic, basic, uncharged

85
Q

Acidic polar amino acids

A

aspartic acid and glutamic acid

86
Q

Basic polar amino acids

A

arginine, histidine, lysine

87
Q

Uncharged polar amino acids

A

asparagine, cysteine, glutamine, serine, theronine, tyrosine

88
Q

Nonpolar amino acids

A
  • usually only have carbon and hydrogen in R groups EXCEPT TRYPTOPHAN AND METHIONINE
  • alanine, glycine, isoleucine, leucine, methionine, phenylalanine, proline, tryptophan, valine.
89
Q

Location of amino acids

A
  • non polar are in the core of soluble proteins
  • clump together
  • clumping makes more stable
  • membrane associated proteins have non polar exposed to interact with non polar fatty acids

-polar amino acids are on the outside of proteins in aqueous environment

90
Q

Branched-chain amino acids

A
  • isoleucine, leucine, valine

- maple syrup urine disease

91
Q

Phenylalanine special sig

A
  • normally is converted to tyrosine

- when defective, you get build up of phe and suffer from PKU

92
Q

Tryptophan special sig

A
  • precursor for serotonin

- pain, sleep, appetite, temp, blood pressure, mood

93
Q

Glysine special sig

A
  • orteogenesis imperfecta
  • collagen always has gly at beginning of sequence (every three) so when it is replaced you get blue eyes and brittle bones
94
Q

Proline special sig

A

-rigid structure

95
Q

Methionine special sig

A

-methyl group donor in methylation reactions

96
Q

amino acids with hydroxyl groups that can be phosphorylated

A
  • serine,threonine,tyrosine
  • contribute to activity of an enzyme
  • can contribute to signal transduction
97
Q

Disulfide bonds

A
  • 2 cys residues interact to form disulfide bond

- strength of overall structure

98
Q

glycosidic bonds

A
  • asn can link to N
  • ser and thr can link to O
  • attach sugars to make glycoproteins
  • important: cell surface recognition, matrix, mucins(protective digestive tract proteins)
99
Q

Histones

A
  • lys and arg

- bind to DNA

100
Q

Histidine special sigs

A
  • precursor to histamine
  • gastric acid secretion
  • inflammatory response
101
Q

Tyrosine special sig

A
  • precursor to catecholamines (dopamine, epinephrine, norepinephrine)
  • dopamine and norepi are NT
  • epi and norepi regulate carbohydrate and lipid metabolism
102
Q

protein folding defects

A
  • genetic mutations
  • age related cellular inefficiencies
  • environmental/ nutritional abnormalities
103
Q

peptide bond

A
  • bond between carboxyl group and amino group of two amino acids
  • NO R GROUPS INVOLVED
  • rigid af
104
Q

primary structure

A
  • sequence of amino acids
  • N terminis and C terminis
  • joined by peptide bonds
  • bond is polar
105
Q

Secondary structure

A
  • hydrogen bonding between the polar peptide bonds
  • R groups do not participate in hydrogen bond
  • alpha helix and beta sheet
106
Q

alpha helix

A
  • due to polar nature of peptide bond
  • oxygen has the partial negative and H has the partial positive
  • R groups extend outward from core
  • R groups are relatively close
  • RIGID PROLINE AND BULKY R GROUPS FORM KINK
107
Q

Beta sheet

A
  • due to polar nature of peptide bond
  • hydrogen bonds form between sections of the peptide that fold back on each other
  • peptide segments are stretched out
  • hydrogen bonds are perpendicular to peptide bonds
108
Q

Tertiary structure

A
  • final three-dimensional form of single polypeptide
  • interactions between R groups
  • can be the r groups of primary structure of domains of secondary
109
Q

4 interactions involved in tertiary structure

A
  • disulfide bonds(stability)
  • hydrophobic interactions(non-non)
  • hydrogen bonds(partial charge-partial charge)
  • ionic bonds(full charge-opposite full charge)
110
Q

Quaternary structure

A
  • only present in proteins having more than one polypeptide chain
  • some proteins have multiple copies of same peptide
111
Q

Name 3 types of anhydrides

A

organic-2 carboxyllic acids
mixed- 1 carboxyllic and 1 phosphoric acid
phosphoric- both phosphoric

112
Q

Thioester composition

A

acid+sulfahydrl group

113
Q

Amide composition

A

-acid+amine

114
Q

Phosphoanhydride composition

A

-phosphoric acid and alcohol

Bichem (9 decks)

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