quiz one essentials Flashcards
Fatty acid composition
long hydrocarbon chains with terminal carboxylic acids
Amino acid composition
amino and carboxylate groups
triglycerol composition
3 fatty acid chains liked to glycerol by ester bonds
Protein composition
amino acid liked via amide peptide bond
Ester composition
acid and alcohol
Name the 3 ketone bodies
Acetoacetate, acetone(volatile), 3-hydroxybutyrate
Name body composition in regards to macromolecules
water protein lipids calcium phosphate carbohydrates nucleic acids
draw functional groups
do it
compare glucose and fructose
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
ATP
2 phosphoanhydride
1 phosphomonoester
1 glycosidic bond
2 alcohol groups
ADP is same but only one phosphoanhydride bond
glycerol
3 OH groups on carbon chain
Pyruvate and lactate
pyruvate (has alpha ketone)
lactate(has alpha hydroxy group)
What atoms have high electron affinity?
N,O,S
Polar and non polar
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
Water and polarity things
- 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
hydrophillic molecules
- 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.
hydrophobic molecules
- molecules with no charge (non polar)
- cannot interact with charges of water
- are soluble in fats because like dissolves like
solubility rule of thumb
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
Amphipathic molecules
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)
Phosphate transfer reaction
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
Phosphate cleavage reaction
phosphate is removed from a compound
- enzyme used to dephosphorylate is phosphatase
- bond is hydrolyzed to inorganic phosphate
rearrangement reactions
bonding pattern within a compound undergoes rearrangement but the overall molecule formula is the same
- structural isomers
- help make it fit for an enzyme
Condensation reactions
condensation of two molecules to form one molecule
- biproduct is water
- requires energy
Hydrolysis reactions
disassembly of polymers to their monomeric units
-requires water, not energy
Oxidation reactions
Loss of hydrogen atoms/ gain of oxygen atoms
- dehydrogense is enzyme that removes 2 hydrogens
- oxidase is enzyme that adds 1 oxygen
Reduction reactions
Gain of hydrogen atoms/ loss of oxygen atoms
-reductase is addition of 2 hydrogen atoms
Acid/ Base reactions
- most biochemical reactions occur in water
- acid releases proton and base accepts proton
- strong acids completely dissociate in water (no pka)
- weak acids partially dissociate (have pka)(how much they dissociate depends on the environment
pH and hydrogen concentration
more acid means lower pH which means more H concentration
Strong/Weak acids
strong acids completely dissociate (no pKa)
weak acids patially dissociate (pKa)
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
pKa range fro carboxylic acids and ammonium ions
pKa for carboxyllic acid: 2-7
pKa from ammonium ion: 6-11
(when they are deprotonated)
Carboxyllic acid deprotonation
unchargerd (RCOOH) to charged (RCOO-)
-uncharged acidic form
Ammonium ion deprotonation
charged (RNH3+) to uncharged (RNH2)
-charged acidic form
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
Henderson-Hasselbach equation
pH=pKa+log(conjugate base)/(acid)
When is a drug absorbed
uncharged form is absorbed
-charged from is not absorbed
name the 2 factors that determine buffer effectiveness
- the buffers pH range
2. the buffers concentration (buffering capacity)
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
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.
G-protein coupled receptor
- extracellular ligand binding domain
- seven transmembrane spanning domain(helices)
- G-protein activation domain
G-protein
- heteromeric (large)
- Beta, gamma, and alpha subunits
Beta and gamma G-protein subunits
-act as membrane localized docking site for inactve alpha subunit
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
Adenylyl cyclase
- integral membrane enzyme
- activated by Galpha protein
- hydrolyzes ATP to get cAMP
cAMP
- cyclic adenosine monophosphate
- second messenger for intercellular signalling
- interacts with protein kinase A
Protein Kinase A
- enzyme made of 2 regulatory subunits and 2 catalytic subunits
- regulatory subunits interact with cAMP and release catalytic subunits
- cAMP dependent
Protein Kinase A catalytic subunits
- phosphorylate target proteins and enzymes
- make them function as intracellular effectors drivin by extracellular signals
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
Protein phosphatase
- enzymes
- hydrolytically cleave phosphate esters
- dephosphorylate effector proteins that were phosphorylated by protein kinase A
cAMP phosphodiesterase
- enzyme
- converts cAMP to 5’AMP which is not a signaling protein
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
Gq protein
- hormone (epinephrine) receptor activated
- interacts with phospholipase C
Phospholipase C
- membrane localized
- cleaves lipid bi-layer
- PIP2 to IP3 and DAG
PIP2
- phosphatidylinositol 4,5-bisphosphate
- membrane phospholipid
IP3
- Inositol 1,4,5-triphosphate
- binds to ER receptor
- activates Ca2+ channels
- releases Ca2+ into cytosol
DAG
- Diacylglycerol
- remains in the membrane
- activates protein kinase C
Protein Kinase C
- cAMP independent
- phosphorylates proteins
- activated by Ca2+ and DAG
Ligands that stimulate IP3 and DAG signaling
- neurotransmitters
- hormones
- growth factors
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
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
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
Glucose stimulation of insulin
- increase in blood glucose results in increase of insulin release
- beta cells produce more insulin
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
gastrointestinal stimulation of insulin
-peptide hormones are released from small intestine as anticipatory insulin release stimulators in response to food intake
Factors that negatively affect insulin secretion
- scarcity of dietary fuels
- increase in epinephrine levels
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
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
Gluc4
- insulin sensitive glucose transporter
- primarily found in muscle and adipose tissue
mechanism of glucose transporter
- glucose transporters move from cell membrane to intracellular storage pool
- vesicles fuse to form endosome
How long does it take to transport glucose into muscle and adipose tissue?
seconds
How long does it take for insulin induced changes in enzymatic activity to occur?
minutes-hours
How long does it take for production of enzymes in response to insulin?
hours-days
Insulin sensitive
skeletal muscle and adipose tissue
Insulin insensitive
active transport: epithelia of intestine, renal tubes, choroid plexus
facilitated transport: lens of cornea, liver, brain, leukocytes
Gycogenesis
- insulin receptor on
- glucose-glycogen
Gycogenolysis
- glucagon and epinephrine on
- glycogen-glucose
Gluconeogenesis
- glucagon and epinephrine on
- non carbohydrate source-glucose
glucagon secretion stimulus
- increased amino acids
- increased epinephrine levels
glucagon signaling
SAME AS CAMP SIGNALING
effects of glucagon signaling
- rise in blood glucose
- activates lipolysis in adipose
- amino acid uptake in liver
ketogenesis
- break down of amino acids to form ketone bodies
- glucagon and epinephrine up
lipolysis
- break down of fats to make fatty acids
- glucagon and epinephrine up
Amino Acid structure
- carbon atom, amino group, carboxylic acid, single hydrogen
- R group gives distinction
Polar amino acids
-acidic, basic, uncharged
Acidic polar amino acids
aspartic acid and glutamic acid
Basic polar amino acids
arginine, histidine, lysine
Uncharged polar amino acids
asparagine, cysteine, glutamine, serine, theronine, tyrosine
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.
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
Branched-chain amino acids
- isoleucine, leucine, valine
- maple syrup urine disease
Phenylalanine special sig
- normally is converted to tyrosine
- when defective, you get build up of phe and suffer from PKU
Tryptophan special sig
- precursor for serotonin
- pain, sleep, appetite, temp, blood pressure, mood
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
Proline special sig
-rigid structure
Methionine special sig
-methyl group donor in methylation reactions
amino acids with hydroxyl groups that can be phosphorylated
- serine,threonine,tyrosine
- contribute to activity of an enzyme
- can contribute to signal transduction
Disulfide bonds
- 2 cys residues interact to form disulfide bond
- strength of overall structure
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)
Histones
- lys and arg
- bind to DNA
Histidine special sigs
- precursor to histamine
- gastric acid secretion
- inflammatory response
Tyrosine special sig
- precursor to catecholamines (dopamine, epinephrine, norepinephrine)
- dopamine and norepi are NT
- epi and norepi regulate carbohydrate and lipid metabolism
protein folding defects
- genetic mutations
- age related cellular inefficiencies
- environmental/ nutritional abnormalities
peptide bond
- bond between carboxyl group and amino group of two amino acids
- NO R GROUPS INVOLVED
- rigid af
primary structure
- sequence of amino acids
- N terminis and C terminis
- joined by peptide bonds
- bond is polar
Secondary structure
- hydrogen bonding between the polar peptide bonds
- R groups do not participate in hydrogen bond
- alpha helix and beta sheet
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
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
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
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)
Quaternary structure
- only present in proteins having more than one polypeptide chain
- some proteins have multiple copies of same peptide
Name 3 types of anhydrides
organic-2 carboxyllic acids
mixed- 1 carboxyllic and 1 phosphoric acid
phosphoric- both phosphoric
Thioester composition
acid+sulfahydrl group
Amide composition
-acid+amine
Phosphoanhydride composition
-phosphoric acid and alcohol
