quiz one essentials Flashcards
(114 cards)
1
Q
Fatty acid composition
A
long hydrocarbon chains with terminal carboxylic acids
2
Q
Amino acid composition
A
amino and carboxylate groups
3
Q
triglycerol composition
A
3 fatty acid chains liked to glycerol by ester bonds
4
Q
Protein composition
A
amino acid liked via amide peptide bond
5
Q
Ester composition
A
acid and alcohol
6
Q
Name the 3 ketone bodies
A
Acetoacetate, acetone(volatile), 3-hydroxybutyrate
7
Q
Name body composition in regards to macromolecules
A
water protein lipids calcium phosphate carbohydrates nucleic acids
8
Q
draw functional groups
A
do it
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
10
Q
ATP
A
2 phosphoanhydride
1 phosphomonoester
1 glycosidic bond
2 alcohol groups
ADP is same but only one phosphoanhydride bond
11
Q
glycerol
A
3 OH groups on carbon chain
12
Q
Pyruvate and lactate
A
pyruvate (has alpha ketone)
lactate(has alpha hydroxy group)
13
Q
What atoms have high electron affinity?
A
N,O,S
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
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
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.
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
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
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)
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
21
Q
Phosphate cleavage reaction
A
phosphate is removed from a compound
- enzyme used to dephosphorylate is phosphatase
- bond is hydrolyzed to inorganic phosphate
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
23
Q
Condensation reactions
A
condensation of two molecules to form one molecule
- biproduct is water
- requires energy
24
Q
Hydrolysis reactions
A
disassembly of polymers to their monomeric units
-requires water, not energy
25
Oxidation reactions
Loss of hydrogen atoms/ gain of oxygen atoms
- dehydrogense is enzyme that removes 2 hydrogens
- oxidase is enzyme that adds 1 oxygen
26
Reduction reactions
Gain of hydrogen atoms/ loss of oxygen atoms
| -reductase is addition of 2 hydrogen atoms
27
Acid/ Base reactions
1. most biochemical reactions occur in water
2. acid releases proton and base accepts proton
3. strong acids completely dissociate in water (no pka)
3. weak acids partially dissociate (have pka)(how much they dissociate depends on the environment
28
pH and hydrogen concentration
more acid means lower pH which means more H concentration
29
Strong/Weak acids
strong acids completely dissociate (no pKa)
| weak acids patially dissociate (pKa)
30
Ka/pKa
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
31
pKa range fro carboxylic acids and ammonium ions
pKa for carboxyllic acid: 2-7
pKa from ammonium ion: 6-11
(when they are deprotonated)
32
Carboxyllic acid deprotonation
unchargerd (RCOOH) to charged (RCOO-)
| -uncharged acidic form
33
Ammonium ion deprotonation
charged (RNH3+) to uncharged (RNH2)
| -charged acidic form
34
concentration trends of conjugate bases and weak acids according to pKa and pH
- when pH=pKa, conjugate base=weak acid concentration
- when pH>pKa, conjugate base>acid concentration
- when pH
35
Henderson-Hasselbach equation
pH=pKa+log(conjugate base)/(acid)
36
When is a drug absorbed
uncharged form is absorbed
| -charged from is not absorbed
37
name the 2 factors that determine buffer effectiveness
1. the buffers pH range
| 2. the buffers concentration (buffering capacity)
38
pH range of a buffer
+/- one pH unit from the pKa of the weak acid
| -pKa is 4, effective range is 3 and 5 is effective pH range
39
Addition of acid/ base to buffer
- 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.
40
G-protein coupled receptor
- extracellular ligand binding domain
- seven transmembrane spanning domain(helices)
- G-protein activation domain
41
G-protein
- heteromeric (large)
| - Beta, gamma, and alpha subunits
42
Beta and gamma G-protein subunits
-act as membrane localized docking site for inactve alpha subunit
43
alpha subunit of G-protein
-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
44
Adenylyl cyclase
- integral membrane enzyme
- activated by Galpha protein
- hydrolyzes ATP to get cAMP
45
cAMP
- cyclic adenosine monophosphate
- second messenger for intercellular signalling
- interacts with protein kinase A
46
Protein Kinase A
- enzyme made of 2 regulatory subunits and 2 catalytic subunits
- regulatory subunits interact with cAMP and release catalytic subunits
- cAMP dependent
47
Protein Kinase A catalytic subunits
- phosphorylate target proteins and enzymes
| - make them function as intracellular effectors drivin by extracellular signals
48
intracellular effectors
- 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
Protein phosphatase
- enzymes
- hydrolytically cleave phosphate esters
- dephosphorylate effector proteins that were phosphorylated by protein kinase A
50
cAMP phosphodiesterase
- enzyme
| - converts cAMP to 5'AMP which is not a signaling protein
51
Vibrio Cholera
- 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
Gq protein
- hormone (epinephrine) receptor activated
| - interacts with phospholipase C
53
Phospholipase C
- membrane localized
- cleaves lipid bi-layer
- PIP2 to IP3 and DAG
54
PIP2
- phosphatidylinositol 4,5-bisphosphate
| - membrane phospholipid
55
IP3
- Inositol 1,4,5-triphosphate
- binds to ER receptor
- activates Ca2+ channels
- releases Ca2+ into cytosol
56
DAG
- Diacylglycerol
- remains in the membrane
- activates protein kinase C
57
Protein Kinase C
- cAMP independent
- phosphorylates proteins
- activated by Ca2+ and DAG
58
Ligands that stimulate IP3 and DAG signaling
- neurotransmitters
- hormones
- growth factors
59
Calcium signaling
- 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
Insulin
- 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
Glucagon
- 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
Glucose stimulation of insulin
- increase in blood glucose results in increase of insulin release
- beta cells produce more insulin
63
Amino acid stimulation of insulin
- 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
gastrointestinal stimulation of insulin
-peptide hormones are released from small intestine as anticipatory insulin release stimulators in response to food intake
65
Factors that negatively affect insulin secretion
- scarcity of dietary fuels
| - increase in epinephrine levels
66
Epinephrine
- 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
Insulin binding
- 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
Gluc4
- insulin sensitive glucose transporter
| - primarily found in muscle and adipose tissue
69
mechanism of glucose transporter
1. glucose transporters move from cell membrane to intracellular storage pool
2. vesicles fuse to form endosome
70
How long does it take to transport glucose into muscle and adipose tissue?
seconds
71
How long does it take for insulin induced changes in enzymatic activity to occur?
minutes-hours
72
How long does it take for production of enzymes in response to insulin?
hours-days
73
Insulin sensitive
skeletal muscle and adipose tissue
74
Insulin insensitive
active transport: epithelia of intestine, renal tubes, choroid plexus
facilitated transport: lens of cornea, liver, brain, leukocytes
75
Gycogenesis
- insulin receptor on
| - glucose-glycogen
76
Gycogenolysis
- glucagon and epinephrine on
| - glycogen-glucose
77
Gluconeogenesis
- glucagon and epinephrine on
| - non carbohydrate source-glucose
78
glucagon secretion stimulus
- increased amino acids
| - increased epinephrine levels
79
glucagon signaling
SAME AS CAMP SIGNALING
80
effects of glucagon signaling
- rise in blood glucose
- activates lipolysis in adipose
- amino acid uptake in liver
81
ketogenesis
- break down of amino acids to form ketone bodies
| - glucagon and epinephrine up
82
lipolysis
- break down of fats to make fatty acids
| - glucagon and epinephrine up
83
Amino Acid structure
- carbon atom, amino group, carboxylic acid, single hydrogen
| - R group gives distinction
84
Polar amino acids
-acidic, basic, uncharged
85
Acidic polar amino acids
aspartic acid and glutamic acid
86
Basic polar amino acids
arginine, histidine, lysine
87
Uncharged polar amino acids
asparagine, cysteine, glutamine, serine, theronine, tyrosine
88
Nonpolar amino acids
- usually only have carbon and hydrogen in R groups EXCEPT TRYPTOPHAN AND METHIONINE
- alanine, glycine, isoleucine, leucine, methionine, phenylalanine, proline, tryptophan, valine.
89
Location of amino acids
- 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
Branched-chain amino acids
- isoleucine, leucine, valine
| - maple syrup urine disease
91
Phenylalanine special sig
- normally is converted to tyrosine
| - when defective, you get build up of phe and suffer from PKU
92
Tryptophan special sig
- precursor for serotonin
| - pain, sleep, appetite, temp, blood pressure, mood
93
Glysine special sig
- 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
Proline special sig
-rigid structure
95
Methionine special sig
-methyl group donor in methylation reactions
96
amino acids with hydroxyl groups that can be phosphorylated
- serine,threonine,tyrosine
- contribute to activity of an enzyme
- can contribute to signal transduction
97
Disulfide bonds
- 2 cys residues interact to form disulfide bond
| - strength of overall structure
98
glycosidic bonds
- 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
Histones
- lys and arg
| - bind to DNA
100
Histidine special sigs
- precursor to histamine
- gastric acid secretion
- inflammatory response
101
Tyrosine special sig
- precursor to catecholamines (dopamine, epinephrine, norepinephrine)
- dopamine and norepi are NT
- epi and norepi regulate carbohydrate and lipid metabolism
102
protein folding defects
- genetic mutations
- age related cellular inefficiencies
- environmental/ nutritional abnormalities
103
peptide bond
- bond between carboxyl group and amino group of two amino acids
- NO R GROUPS INVOLVED
- rigid af
104
primary structure
- sequence of amino acids
- N terminis and C terminis
- joined by peptide bonds
- bond is polar
105
Secondary structure
- hydrogen bonding between the polar peptide bonds
- R groups do not participate in hydrogen bond
- alpha helix and beta sheet
106
alpha helix
- 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
Beta sheet
- 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
Tertiary structure
- final three-dimensional form of single polypeptide
- interactions between R groups
- can be the r groups of primary structure of domains of secondary
109
4 interactions involved in tertiary structure
- disulfide bonds(stability)
- hydrophobic interactions(non-non)
- hydrogen bonds(partial charge-partial charge)
- ionic bonds(full charge-opposite full charge)
110
Quaternary structure
- only present in proteins having more than one polypeptide chain
- some proteins have multiple copies of same peptide
111
Name 3 types of anhydrides
organic-2 carboxyllic acids
mixed- 1 carboxyllic and 1 phosphoric acid
phosphoric- both phosphoric
112
Thioester composition
acid+sulfahydrl group
113
Amide composition
-acid+amine
114
Phosphoanhydride composition
-phosphoric acid and alcohol
