Bio/Biochem Flashcards
Where is growth hormone released from?
anterior pituitary gland
where is ghrelin released from, what does it act on, and what does it result in?
released from the stomach cells it is a gut hormone, that acts on the hypothalamus, and stimulates appetite (think food gremlin)
what is a tropic hormone
a hormone that targets endocrine cells and stimulates the release of other hormones
Opposite of direct!!
what is a steroid hormone
a group of hormones derived from cholesterol that act as chemical messengers in the body
What happens in G0 phase
resting phase, is the phase of the cell cycle during which a cell isn’t dividing or preparing to divide
what are the three main components of intercellular scaffolding
microfilaments, intermediate filaments, and microtubules
What do microtubules do?
regulate cell growth and movement
which direction does kinesin transport? Dynein?
kinesin: nucleus-> distant
dynein: distant->nucleus
D first, Dynein/Distant
what 3 things help maintain resting potential
passive transport, active transport, membrane selective permeability
how are substances filtered through the glomerular capillaries?
by size
If something is in the proximal convoluted tubule, was it filtered as the glomerulus
Yes- just have been small enough to pass through glomerulus to make it to PCT
what do hot temperatures cause? Cold temperatures?
Vaso____ and vaso____
hot- vasodilation
cold-vasoconstriction
what is the outermost layer of skin
epidermis
what is the most superficial layer of the epidermis
stratum corneum
what is the stratum corneum composed of and what purpose does it do?
Keratinocytes; barrier against external pathogen invasion, prevent water and salt loss thru skin surface
How does Ca 2+ work in muscle contraction?
Ca2+ binds to troponin-> troponin moves tropomyosin-> myosin moves actin
ca-tropo-tropomyo-myo
what does skeletal muscle contraction do to veins? Blood delivery to the heart?
Compress veins, increase the delivery of venous blood to the heart
which amino acid has an R-configuration?
cysteine
How do you calculate pI of arginine?
It’s basic, so
(pka NH3+ + pka R-group)/2
How do you calculate pI or Aspartic acid
It’s acidic so
(pka COOH +pka r-group)/2
How do you calculate pka from valine?
It’s non-polar/uncharged so
(pka COOH + pka NH3+)//2
What molecule is released during the formation of a peptide bond
H2O
What is the difference between an oligopeptide and polypeptide
oligopeptide= few (or any less than 20 but greater than 1 amino acid)
polypetide= many (more than 20)
what role does proline play in secondary structures
proline has a rigid structure, causes it to induce kinks in alpha-helices or turn in Beta sheets
what are stabilizing bonds of tertiary structures (4)?
van der waals forces
hydrogen bonds
ionic bonds
covalent bonds
What are three different prosthetic groups and what are the names of the conjugated proteins?
prosthetic groups: lipids, nucleic acids, carbohydrates
conjugated protein: lipoprotein, glycoprotein, nucleoproteins
How does heat work to denature proteins?
increase average kinetic energy->disrupting hydrophobic interactions and other weak forms of bonding
how do solutes work to denature proteins?
disrupt bond folding: secondary, tertiary, and quaternary structure
The conversion of ATP to cyclic AMP and inorganic phosphate is most likely catalyzed by which class of enzyme
Lyase
How does gel electrophoresis separate out molecules
by molecule weight
What two metabolic pathways are activated to increase the production of glucose?
glycogenolysis and gluconeogenesis
what also is produced when Succinyl-CoA is converted to succinate in the citric acid cycle?
One NTP
How many NAD+ are consumed when glucose is converted to two acetyl-CoA molecules?
4
Michaelis-menten equation
what shift on a line weaver burke plot would show decreased Km and Vmax?
Catalysts do no effect…
equilibrium concentrations
increasing the amount of enzyme available has what effect on Vmax and Km?
increase Vmax
no change to Km
Which is the only R-configuration amino acid?
Cysteine
What are the 4 basic steps of every blotting technique?
- Gel electrophoresis to separate by size
- transfer from gel to membrane
- addition of probe
- visualization of probe
Which amino acids are the most common sites of phosphorylation? Why?
Serine, Threonine, and tyrosine because of their hydroxyl groups
what is collagen’s structure and where is it found?
trihelical structure (3 left handed helices woven together) and mostly found in extracellular matrix
Where is elastin found and what is it important for?
`extracellular matrix of connective tissue, stretches and recoils like a spring to help restore original shape of tissue
Keratins are in what category and what do they mostly make up?
They are intermediate filaments and make up hair and nails
What does actin make up in myofibrils?
microfilaments and the thin filaments in myofibrils
What is a key feature of actin’s structure and how does it aid in transport?
They are polar with a positive and negative side; allowing motor proteins to travel along it unidirectionally
Tubulin is the protein that makes up
microtubules
What role does myosin play in myofibrils?
Thick filament
What class of protein are cadherins?
cell adhesion molecules; hold 2 cells of the same or similar type together
What are 3 types of cell adhesion molecules (CAMs)
cadherins, integrins, and selectins
What is the most common protein in immune response?
antibodies (aka immunoglobulins)
Where are antibodies produced? What do they do?
They’re produced in B-cells, and they neutralize tragets like bacteria and toxins and recruit other cells to help eliminate the threat
What is the structure of antibodies?
Y-shaped, two heavy chains and two light chains that are bound together thru cysteine bonds
When antibodies bind to antigens what are three potential outcomes?
1) Neutralize it -can’t exert any more effect on the body
2)Opsonization-mark it to be destroyed by other white blood cells
3)agglutinating- stay connected and clump together to then be phagocytized by macrophages
Are motor proteins catalytic?
Yes- because of the ATPase activity that they display
What type of adhesion does integrin aid in?
cell to protein in the extracellular matrix
What type of adhesion does selectin aid in?
cell to carbohydrates (usually on the surface of other cells)
What are the three types of G proteins in protein-coupled receptors/what they do?
Gs: Stimulates adenylate cyclase which increases cAMP in cell
Gi: Inhibits adenylate cyclase which decreases cAMP in the cell
Gq: activates phospholipase c
Gs: Stimulate
Gi: inhibit
Gq: mind your ps and qs- q activates phospholipase c
What 3 physical characteristics do both enzyme-linked receptors and G-protein coupled receptors both display?
- contain extracellular domain
- contain transmembrane domain
- Ligand binding
What type of ion channel is always open? Example
ungated channels; potassium channels
Electrophoresis general overview
Used to separate proteins
Attached to battery; anode and cathode
gel is normally polyacrylamide gel
travel based on size and charge
How does isoelectric focusing separate proteins?
Based on their pI; moves toward electrode until it reaches region of gel where pH=pI of protein
Native PAGE vs SDS PAGE
Native maintains protein shape, but results are difficult to compare b/c of mass-to-charge ratios differing
SDS denatures and makes size comparison more accurate, but cannot make that protein functional again
In size-exclusion chromatography which molecules elute first and why
large ones, because the smaller ones get trapped in small pores
what two factors have a role in how fast a protein moves in column chromatography
size and polarity
What are two methods used to determine protein structure? Which is the most popular?
Xray crystallography (most popular)
NMR spectroscopy
how can amino acid composition be determined?
could be by simple hydrolysis, but sequencing requires sequential degradation, like Edman degradation
What are the two colors of Bradford protein assays? What do they show
Starting color is a brown-green hue, if increased protein concentration is, then will turn to blue.
More blue=more protein
At what pH would one protein be best separated from two others with higher pIs in electrophoresis?
At a pH greater then the proteins pI, but less then the pI of the other two proteins
cell migration:
movement of cells
A hormone found in low concentrations, but has a strong effect would likely act on which types of receptors?
1. Enzyme-linked receptors
2. G protein-coupled receptor
3. Ligand-gated ion channels
- Enzyme-linked receptors
- G protein-coupled receptor
not ligand-gated bc there is no second messenger cascade, so small amount binding could not have a strong effect
Do antibodies bind to 1 or multiple different antigens?
one antigen
what method would be good to separate proteins of different sizes but similar pI?
Size-exclusion chromatography
Which amino acid structures are best used for UV spectroscopy
aromatic ones because of double bonds
How to establish a negative control
keep the conditions almost the same, but the addition of something that is known not to have thee desired effect
What is a parameter in research?
A measure using every person in a population, not of a sample
enantiomers
non-identical mirror image of each other; different chirality
how do you calculate the number of stereoisomers with a common backbone
2^number of chiral centers
diastereomers
two sugars in the same family (same #carbon, either ketoses or aldoses) that are not identical or mirror images
epimers
diastereomers that only differ at one position
What determines the D or L shape of carbohydrates
the -OH closest to the CH2OH group. If to the left=L if to the right=D
Cyclic hemiacetals are formed from
aldoses
Cyclic hemiketals are formed from
ketoses
What is the difference between an aldose and ketone?
Aldose: =O is at the end
Ketone: =O is in the middle
What is the difference between the alpha and beta anomeric forms of glucose?
Alpha= -OH group (that used to carbonyl) is axial and down
Beta=-OH group (that used to carbonyl) is equatorial and up
What is mutarotation in sugars? What is needed
the addition of water to open a hemiacetal chain and convert it to the other anomer (aloha to beta or vice versa)
Lactone sttucture and how it forms
Results from the oxidation of a hemiacetal ring (reducing sugar)
What two reagents can detect the presence of a reducing sugar? What colors do they turn when present
Tollen’s reagent: turns silvery
Tolkein: Silver haired elves
Benedicts reagent: produces solid
Eggs benedict: not runny
saturated vs unsaturated lipid fatty acid chain
saturated: only single bonds
unsaturated: at least one double bond
Sphingolipid structure
Have nitrogen in the backbone (part of sphingosine) rather than straight glycerol. simplest is the ceramide with just a hydrogen head
Isoprene formula and what important lipids they make up
C5H8 and they makeup terpenes and terpenoids
Common steroid structure
3 cyclohexanes and a cyclopentane
what do prostaglandins do, and what effects do they have on the body
They regulate cAMP levels, and effect muscle contraction, body temperature, sleep-wake cycle and fever/ pain
In which main two molecules does the human body store energy? Which is preferred?
Glycogen and triacylglycerols; triacylglycerols are preferred because of the long carbon chain
triglycerol structure
glycerol backbone esterified to three fatty acids
Name of animal cells used for storage of large triacylglycerol
adipocytes
What is the difference between deoxyribose and ribose
deoxyribose lacks an -OH group on the 2’ carbon
The common name for a guanine nucleotide
GTP
The name for an adenosine nucleotide
ATP
What are the names of the 5 important nucleotide/nucleoside bases?
adenine
guanine
cytosine
uracil
thymine
Directionally, How is the sugar-phosphate backbone of DNA formed? Which way is it read?
The 3’ of the carbon of one group to the 5’ phosphate group of the next incoming sugar. It is read 5’ to 3’
Purine structure vs pyrimidine structure
purine= 2 ring, pyriminide=1 ring
What four rules must be satisfied to something to be considered aromatic
- cyclic
- planar
- conjugated
- 4n+2 =pi electrons (huckel’s rule)
Which bases are purines
Guanine and adenine
Which bases are pyrimidines
cytosine, thymine, uracil
What happens when DNA is denatured
the double helix is broken into single strands, but the covalent links between the nucleotides and backbone break
What are common ways to denature DNA
heat, alkaline pH, chemicals like urea
Can denatured DNA be brought back together?
Yes; by reannealing, when the denaturation condition is slowly removed
DNA is wound around ______ forming________
DNA is wound around histones forming chromatin
Nucleosomes are composed of
DNA wrapped around histones They are the rolled film shape, the dna is the the actual film line, and histones are the internal canister that wraps it up
Differences between heterochromatin and euchromatin
heterchromatin: dark, dense, transcriptionally silent
euchromatin: light uncondensed and expressed
Telomeres
located at the end of DNA, high G-C concentration helps prevent unraveling
What happens to telomeres during replication? What enzyme can this be remedied by?
They are shortened; can be reversed by telomerase
centromeres
located in the center of chromosomes and hold sister chromatids together. HIgh GC concentration
During what phase of mitosis are sister chromatids separated
Anaphase
Which enzyme unwinds DNA
Helicase
DNA topoisomerases act by
cuts and then reseals strands to release the tension caused from positive super coiling
Why is DNA replication semiconservative
because each new strand also incorporates one parent strand
DNA polymerases function
read parent strands and generate daughter strands
What is the reading direction of DNA polymerase
3’-5’, but it synthesizes the new strand 5’-3’
Which strand has Okazaki fragments? Why?
Lagging strand, because DNA polymerase “reads” in the 3’ to 5’ direction
Which enzyme joins Okazaki fragments
DNA ligase
Mutations of _______ cause oncogenes
proto-oncogenes
Tumor suppressor genes
code for proteins that reduce cell cycling or promote DNA repair
During which phase of the cell cycle does mismatch repair happen
G2
How does nucleotide excision repair work
fix helix deforming lesions of DNA using excision endonuclease
how to fix thymine dimers
nucleotide excision repair using excision endonuclease
How to fix cytosine deamination
base excision repair using AP endonuclease
Which is not a glycolipid?
a.cerebroside
b.globoside
c.ganglioside
d.sphingomyelin
sphingomyelin; it’s a phospholipid because it doesn’t have a glycosidic bond
Why are triacylglycerols used in the human body for energy storage?
The carbon atoms of fatty acid chains are highly reduced and therefore yield more energy upon oxidation
What vitamin is necessary for the posttranslational introduction of calcium-binding sites
Vitamin K
Saturated or unsaturated make a more fluid solution?
Unsaturated
What inhibits prostaglandin synthesis?
NSAIDs
A 95% confidence interval will fall within what distance from the mean?
=/- 2 sigma
How is cDNA created
the reverse transcription of processed mRNA
What do endonucleases do and what are a couple of things they’re used for
Endonucleases are enzymes that cut DNA
Used for:
DNA repair
Scientists during DNA analyses as restriction enzymes
(cleave DNA before electrophoresis, southern blotting)
During which phase of the cell cycle are DNA repair systems least active?
M
Which enzyme transcribes mRNA from template DNA
RNA polymerase
What enzyme charges or activates tRNA with an amino acid?
aa: aminoacyl-tRNA synthetase
Many rRNA molecules can function as
ribozymes
Where is the wobble position in codons
the third base pair- because changes to it can still result in the same protein (ie be a silent mutation)
3 types of point mutations
silent: nothing happens
missense: 1 aa difference
nonsense: 1 aa difference is a premature stop codon
free card:)
woohoo
The start codon is _____ and codes for_____
AUG-methionine
The 3 stop codons are
UAA
UAG
UGA
U Are ANnoying
U Go Away
U Are Gone
where does RNA polymerase II bind in the promoter region during transcription of mRNA
TATA box
what is the name of the primary transcript formed immediately after transcription
hnRNA; after posttranscriptional processing is mRNA
what two posttranscriptional processes help protect against degradation
addition of 5’ cap and 3’ poly-A-tail
Which type/ of RNA polymerase is associated with which type/types of RNA?
RNA polymerase I: rRNA
RNA polymerase II: mRNA also hnRNA and snRNA
RNA polymerase III: tRNA and some rRNA
where does translation occur
ribosomes
Chaperones
aid in posttranslational protein folding
Name for post-translational addition of lipid groups to membrane-bound enzymes
prenylation
What are the 3 sites of ribosomes important during translation?
APE
A-site
P-site
E-site
lac operon is what type of system?
negative inducible system- under normal conditions turned off, but by removing bound repressor lac operon turns on
trp operon works as what type of system?
negative repressible system- under normal conditions are on, but can be turned off by coupling of repressor and corepressor binding to operator site
Histone acetylation results in
decreased positive charge on lysine residues and weaker interactions of histone with DNA- open chromatin, easier access of transcription
Difference between promoter and enhancer locations in DNA
promoters: within 25 base pairs of the transcription start site
enhancers: more than 25 base pairs from the transcription state site
What role does peptidyl transferase play in protein synthesis
catalyzes the formation of a peptide bond between incoming aa in A site and the growing polypeptide chain in the P site
The promoter is the location of where what binds.
RNA polymerase
Enhancers enhance the activity of
RNA polymerase at a single promoter site
3 types of RNA are found in the spliceosome
snRNA, hnRNA, snRNP
connection of a carboxylate group of one amino acid to a the amino group of an incoming amino acid form what type of bond?
Amide (aka a petpide bond)
What do flippases do?
They help flip lipids from one side of the the membrane through to other (difficult because middle is so hydrophobic)
Lipid rafts
groupings of similar lipids that can serve as attachment points for other biomolecules
List the following from most to least plentiful in the membrane:
Carbs, nucleic acids, proteins, lipids
Lipids, proteins, carbohydrates, nucleic acids
what is one way to visually tell if a fatty acid tail is saturated or unsaturated?
Unsaturated will have a bend or kink in the chain (double bond)
How does cholesterol impact membrane fluidity at high and low temps?
High temps: decreases fluidity
Low temps: increases fluidity
bidirectional!
Gap junctions
Allow direct cell to cell transport of water and some solutes
Tight junctions
physical link between cells as they form a single layer of tissue. DO NOT allow the transport of solutes or water
The formula for osmotic pressure
What thermodynamic factor is primarily responsible for passive transport?
Entroopy
resting membrane potential is least likely to be -75, 0, or +35?
0, because the resting membrane potential
Inner mitochondrial membrane vs outer mitochondrial
inner is much more impermeable and lacks cholesterol
gangliosides are a category of
sphingolipids
Where is GLUT 2 located? km high or low?
hepatocytes and pancreatic cells/ km high
Where is GLUT4 located?km high or low?
adipose tissue and muscle/km low
What is the rate-limiting enzyme of glycolysis
phosphofructokinase-1
What is the rate-limiting enzyme of fermentation
lactate dehydrogenase
What is the rate-limiting enzyme of glycogenolysis
glycogen phophorylase
What is the rate-limiting enzyme of gluconeogenesis
fructose-1,6-biphosphatase
What is the rate-limiting enzyme of the pentose phosphate pathway
glucose-6-phosphate dehydrogenase
When should the cell turn on glycolysis?
when it needs energy (high AMP)
When should the cell turn off glycolysis?
When it has sufficient energy (high ATP)
What do hexokinase and glucokinase do in glycolysis? what is the difference between them?
They both are the first step of glycolysis and convert glucose to glucose-6-phosphate.
Glucokinase is used in the liver rather than hexokinase which is used every where else
What are the differences between hexokinase and glucokinase?
hexokinase: in most tissues, low km, inhibited by glucose-6-phosphate
glucokinase: in hepatocytes and pancreatic B-islets, high km, induced by insulin
What does phosphofructokinase-1 do?
In glycolysis converts fructose-6-phosphate to fructose 1,6-biphosphate using ATP
Insulin _______PFK-1 and glucagon _________PFK-1 in hepatocytes
Insulin stimulates PFK-1 and glucagon inhibits PFK-1 in hepatocytes
What does glyceraldehyde-3-phosphatase do in glycolysis
catalyze the oxidation and inorganic phosphate addition to glyceraldehyde 3-phosphate into 1,3-bisphosphateglycerate
and reduction of NAD+ to NADH
3-phosphoglycerate kinase catalyzes the production of what two things in glycolysis?
1)3-phosphoglycerate
2) ATP
What earlier product of glycolysis activates pyruvate kinase? What is this called?
fructose 1,6-bisphosphate,
called feed-forward activation
What is the key enzyme of fermentation? What does it do
lactate dehydrogenase, and it oxidizes NADH to NAD+
Which glycolysis intermediate can be used for triacylglycerol synthesis in hepatic and adipose tissue?
Dihydroxyacetone phosphate (DHAP)
What are the irreversible enzymes of glycolysis
hexokinase, glucokinase, PFK-1, Pyruvate kinase
How Glycolysis Pushes Forward the Process: Kinases
What is galactose phosphorylated by?
galactokinase, trapping it in cell
What is fructose phosphorylated by?
fructokinase, trapping it in the cell
What are the 3 reactants of the PDH complex?
Pyruvate, NAD+, CoA
What are the 3 products of the PDH complex?
Acetyl-CoA, NADH, and CO2 are the products
What does Pyruvate dehydrogenase do?
Convert pyruvate to acetyl-CoA
What stimulates PDH? What inhibits it?
Stimulates: insulin
Inhibits: acetyl-CoA
Glycogen
A branched polymer of glucose, is a storage form of glucose
How is glycogen used in the liver vs in skeletal muscle?
Liver: glycogen is broken down to maintain levels of glucose
skeletal muscle: glycogen is broken down to provide glucose during vigorous exercise
In what form do plants store excess glucose?
Starch
Glycogenesis
The synthesis of glycogen granules
glycogenolysis
The breaking down of glycogen
Two key enzymes of glycogenesis
- glycogen synthase (a 1-4 links keep extending branches of glycogen)
- Branching enzyme (a 1-6 puts a new branch on glycogen
a-1,4 keeps the same branch moving “4ward”, while a 1-SIX puts a new branch in the MIX
two key enzymes of glycogenolysis
- glycogen phosphorylase (breaks a 1-4 links)
- debranching enzyme (breaksa 1-6 bond)
What are the key counterregulatory hormones to insulin (4)?
glucagon, epinephrine, cortisol, growth hormone
Glucogenic amino acids
can be converted into intermediates that feed into gluconeogenesis
all of them except the Ls leucine and lysine
Which 2 enzymes of gluconeogenesis bypass pyruvate kinase of glycolysis?
Pyruvate carboxylase and PEPCK
Which enzyme of gluconeogenesis bypasses glucokinase? Where is it found?
Glucose-6-phosphatase; found only in the endoplasmic reticulum of the liver
What are the two major metabolic products of the pentose phosphate pathway?
ribose-5-phosphate and NADPH
What are the 3 primary functions of NADPH
- Lipid biosynthesis
- bactericidal bleach formation in white blood cells (helps with bactericidal)
- maintenance of glutathione stores to protect against reactive oxygen species
What four molecules other than pyruvate can be used to make acteyl-CoA
fatty acids, ketogenic amino acids, ketones, alcohol
What is the first step of the citric acid cycle?
Condensation rxn of Acetyl-CoA and oxaloacetate catalyzed by citrate synthase
In the citric acid cycle, isocitrate is oxidized to alpha-ketoglutarate by
isocitrate dehydrogenase
Substrates of the citric acid cycle
Pyruvate
Citrate
Isocitrate
a-ketoglutarate
Succinyl-CoA
Succinate
Fumerate
Malate
Oxaloacetate
Please, Can I Keep Selling Seashells For Money, Officer
from glycolysis thru oxidative phosphorylation, how much ATP is yielded?
32 ATP
What are the 3 checkpoints of the citric acid cycle that can be inhibited or stimulated?
- citrate synthase
- Isocitrate dehydrogenase (RATE LIMITING STEP)
3.a-ketoglutarate dehydrogenase complex
What inhibits citrate synthase?
ATP, NADH, succinyl-CoA, citrate
What inhibits isocitrate dehydrogenase? Stimulates?
Inhibit: ATP, NADH
Stimulate: ADP, NAD+
What are the 4 complexes of the ETC each most responsible for?
Complex I: NADH-> CoQH2 (Co-enzyme Q)
Complex II: Succinate-> CoQH2
Complex III: CoQH2->Cytochrome c
Complex IV:Cytochrome c+ O2->2H2O
Why does cyanide have such an intense effect on the body?
Cyanide attaches to iron group needed for the last step of the ETC (Complex IV) and prevents the transfer of electrons
proton motive force
generated by the ETC, creates an electrochemical gradient across the inner mitochondrial membrane which drives ATP synthase
What are two shuttle methods used to help NADH enter the inner mitochondrial membrane
-malate-aspartate shuttle (more efficient)
-Glycerol-3-phosphate shuttle
Oxidative phosphorylation
The process by which ATP is generated via harnessing the proton gradient and utilizing ATP synthase
which GLUT transporter is used by cells in the liver to store excess glucose and by beta cells in the pancreas as a glucose sensor
GLUT 2
Which organ does not require a constant source of glucose from the blood for energy during a fast?
Liver- it can produce its own glucose through gluconeogenesis
When b-oxidation is predominant, the TCA will shift to do what
Shift backwards to produce oxaloacetate for gluconeogenesis
Citrate is a negative allosteric regulator of what step in glycolysis
phosphofructokinase-1
Does fructose enter glycolysis unstream or downstream of PFK-1?
Downstream
Of glycolysis, TCA, and the ETC which is involved in anaerobic metabolism
Glycolysis