Last Deck is Always the Hugest Flashcards
1
Q
What’s the TCA Cycle specifically looking for?
A
2-carbon units
2
Q
Describe E1 of PDH
A
It’s Pyruvate Dehydrogenase, 24 chains, TPP is it’s prosthetic group, and it catalyzes oxidative decarboxylation of pyruvate
3
Q
Describe E2 of PDH
A
Dihydrolipoyl Transacetylase, 24 chains Lipoamide Prothetic Group, and catalyzes transfer of acetyl group to CoA
4
Q
Describe E3 of PDH
A
It’s Dihydrolipoyl Dehydrogenase, 12 chains long, FAD prosthetic group, and it regenerates the oxidized form of lipoamide
5
Q
What keeps PDH functioning so well
A
It’s proximity of all enzymes increases reaction rates and keeps all intermediates bound. The flexible E2 arm calls on each active site in turn.
6
Q
Step 1 of PDH Cycle?
A
Pyruvate enters
CO2 Leaves. TPP group in E1 chamber Bonds with the…Acetyl group?
7
Q
Step 2 of PDH Cycle?
A
Lipomyl arm swings into TPP E1 group
8
Q
Step 3 of PDH Cycle?
A
Lipomyl arm swings the acetyl group into the E2 group
9
Q
Step 4 of PDH Cycle?
A
CoA enters, Acetyl CoA group leaves, and Oxidized Lipomyl Arm Swings into E3 FAD group
10
Q
Step 5 of PDH Cycle?
A
Regnerated Lipomyl Arm leaves the E3 “chamber”, but now FAD has become FADH2
11
Q
Step 6 of PDH Cycle?
A
NAD+ Comes along and NADH and H+ leaves to set it back to the original FAD and PDH is ready again
12
Q
What inhibits and activates PDH?
A
- PDH is regulated allosterically by reverse phosphorylation.
- Also, High acetyl CoA directly inhibits E2
- Phosphorylated PDH is inactive PDH. Dephosphorylation occurs through phosphotase at the expense of H2O.
- ATP activates KINASE which Deactivates PDH.
- So Indirectly, High Levels of ADP might Indirectly keep PDH active. Same for Pyruvate. High levels of pyruvate activates phosphatases which activate PDH.
- NAD also indirectly activates PDH
- Indirect Inhibitors can include NADH, Acetyl CoA, and ATP.
13
Q
Describe the “3rd” Step of the TCA Cyle
A
- Starting with an Alpha Keto-Glutarate
- Enzyme alpha-ketoglutarate deydrogenase complex
- NAD+ and CoA is taken in.
- NADH, H+, and CO2 leaves
- Succinyl CoA is formed.
- This step is Very similar to PDH.
- Both reactions decarboxylate an alpha-ketoacid and create a thioester linkage with CoA
14
Q
One More Time, just to hammer this bitch home,
Name all of the Activators that assist in sending PDH to it’s INACTIVE state…(PHOSPHORYLATED)
Inhibitors?
A
Activators:
- Acetyl CoA
- NADH
- ATP
Inhibitors:
- ADP
- Calcium
- Pyruvate
- CoA
- NAD+
- H+
15
Q
Now…What are the acivators and inhibitors in sending inactive PDH into it’s ACTIVE state?
A
Activators:
- Calcium
- Magnesium
- NAD+
- CoA
- Insulin
- H+
Inhibitors:
- NADH
- Acetyl-CoA
16
Q
Describe the “4th” step of the TCA cycle
A
- Start with Succinyl CoA
- Enzyme Succinyl CoA Synthetase
- GDP and Pi come in
- GTP and CoA leave
- Product is Succinate.
- This is the only step in the cycle that has a GTP product
- Succinyl CoA contains a high energy thioester bond (Similar to ATP)
17
Q
Describe the 5th Step of the TCA Cycle
A
- Starting with Succinate
- Enzyme Succinate Dehydrogenase
- FAD comes in,
- FADH2 comes out
- Product is Fumarate
- This Fumarate step is apparently quite useful because it produces FADH2. Which we use elsewhere.
18
Q
Describe the “2nd” Step of the TCA Cycle
A
Why didn’t we start with this one? I dunno.
- Starting with Isocitrate
- Enzyme Isocitrate Dehydrogenase
- NAD+ Comes in,
- NADH and H+ Come Out
- Intermediate Product is oxalosuccinate.
- From there, H+ enters, (yes that’s right)
- CO2 leaves
- Ending product is alpha-ketoglutarate
- This one is the first major allosteric control point.
- ADP Activates
- ATP and NADH Inhibit
19
Q
Describe the 1st step of the pentose phosphate pathway
A
- Starting with G-6-P
- Enzyme Glucose 6-phosphate dehydrogenase
- 2 NADP+ enters,
- 2 NADPH and CO2 leave (I think 2 CO2)
- Product is Ribulose 5 phosphate
- PPP Synthesizes Pentoses such as ribose and deoxyribose
- NADPH for reductive biosynthesis such as cholesterol, and glutathione
- This first step is the rate limiting step
20
Q
Why are there multiple modes available for the PPP?
A
Producing NADPH from G6P is an oxidative process, however from F6P, one can nonoxidatively produce Ribulose 5 phosphate without producing any NADPH. This is a Nonoxidative Process.
- Sometimes we need one more than the other
21
Q
When is Mode 1 of PPP used?
A
When much more Ribose 5 phosphate than NADPH is required, we skip the oxidative step and product Ribose 5-phosphate from Fructose 6 phosphate
22
Q
When is Mode 2 of PPP used?
A
When an equal number of NADPH and Ribose 5-phosphate are required,
- The Normal Mode. Oxidatively converts G6P to Ribulose-5-phosphate producinig 2 NADPH
23
Q
When is Mode 3 of PPP Used?
A
When More NADPH than R5P is required
- In this step, R5P is converted into Glyceraldehyde 3 phosphate, which sends that up the chain to Produce more G6P.
- From there, another oxidative cycle of producing NADPH can occur.
24
Q
When is Mode 4 of PPP Used?
A
When there is a need for both NADPH and ATP.
- Similar to Mode 3, R5P is converted to Glyceraldehyde 3-phosphate.
- Glyceraldehyde 3 phosphate goes down the glycolysis chain to produce more Pyruvate (Gaining 2 ATP)
25
Describe what disorder is found in the Pentose Phosphate Pathway
- Not sure what this deficiency is called...
- But it's X-linked. So more men get it.
- Causes Hemolytic Anemia because of Deficient levels of NADPH in red cells.
- I guess it's just called G6PD deficiency, or Glucose 6 phosphate dehydrogenase deficiency
- So in failing to produce NADPH because of shitty enzymes...
- This shitty enzyme is inhibited by low levels of NADPH. It's supposed to be activated I think.
- Without NADPH, Glutathione reductase can't reduce Oxidized Glutathione (GSSG) down to Reduced Glutathione (GSH).
- Reduced Glutathione is needed to maintain healthy red cell membranes
26
Describe's insulin's effect on Glucose
- Activates Glucose (GLUT4), causing increased glucose uptake in muscle and adipose
- Activates Glucokinase, which increases glucose uptake in the liver
27
Describe insulin's effect on glycogen
- Activates Glycogen Synthase, which increases glycogen synthesis in the liver and muscle
- Inhibits Glycogen Phosphorylase, Which in turn Decreases Glycogen Breakdown in the liver and muscle.
28
Describe insulin's effect on glycolysis
Activates PFK-1 (by PFK-2), and activates PDH complex, which increases Glycolysis and Acetyl-CoA production in the liver and muscle.
29
Describe insulin's effect on fatty acids
- Activates Acetyl CoA Carboxylase, which increases fatty acid synthesis in the Liver.
- Activates Lipoprotein Lipase, which increases Triacylglycerol synthesis in adipose tissue.
30
What can an insulin deficiency or resistance cause?
Hyperglycemia, metabolic syndrome, and diabetes
31
Describe the Physiological effects of epinephrine
Increases Heart Rate
+ Increases Blood Pressure
+ Increases Dilation of Respiratory Passages
= Increased delivery of Oxygen to muscle tissues
32
Describe the metabolic effects of epinephrine pertaining to Glucose
Increases:
- Glycogen Breakdown in the muscle and Liver
- Gluconeogenesis in the liver
Decreases:
- Glycogen Synthesis in the muscle and liver
Overall: Increases Production of Glycose for Fuel
33
Describe the metabolic effects of epinephrine pertaining to ATP
Increases Glycolysis in the muscle,
| which increases ATP production in the muscle
34
Describe the metabolic effects of epinephrine pertaining to fatty acids.
Increases Fatty Acid Mobilization in adipose tissue
Which increases availability of fatty acids as fuel
35
Describe the metabolic effects of epinephrine influence other hormones
I may have worded that question wrong but...
- Increases Glucagon Secretion
- Decreases Insulin Secretion
Which overall reinforce the metabolic effects of epinephrine.
36
Describe Glucagon's effects on glycogen?
- Activatess Glycogen Phosphorylase (Which increases Glycogen breakdown in the liver into glucose)
- Inhibits Glycogen Synthase (Which decreases glycogen synthesis in the liver so less glucose is stored as glycogen)
37
Describe glucagon's effects on Glucose Production (Directly)
- Inhibits PFK-1 (Which decreases glycolysis in the liver so that less glucose is used as fuel)
- Inhibits Pyruvate Kinase...
- But Activates FBPase-2 and PEP carboxykinase (All three of which increase gluconeogenesis in the liver so that amino acids, glycerol, and oxaloacetate are used to produce more glucose)
38
Describe Glucagon's effect on fatty acids
Activates Triacylglycerol lipase and Perilipin Phosphorylation (Which increases fatty acid mobilization in adipose tissue so that less glucose is used as fuel by liver and muscle)
39
Describe glucagon's effect on ketones
Activates acetyl-CoA Carboxylase, which increases ketogenesis and provides an alternative to glucose as an energy source for the brain.
40
Why do some people get fat
Short version: Leptin is a hormone that bonds to receptors in cells telling it "You're Not Hungry".
- It's done by SOCS
- SOCS means Supproessors of Cytoking Signalling.
- SOCS disrupt interactions of of components of insulin signaling and inhibit insulin from fully working "cuz it doesn't need to"
- I'm unclear as to where leptin get's involved, but he compares it to SOCS prohibiting insulin from working to consume energy.
41
What occurs when you're in a well-fed state?
Pancreas detect glucose in the portal vein, and release insuliin. (You should know what happens after that).
- Also Triacylglycerides are broken down into chylomicrons which enter liver and occasionally muscle.
- VLDL can leave the liver to go to adipose tissue or sometimes muscle.
42
What occurs when you're in an extended fasting state?
Pancreas detect "no glucose" in the portal veins and secrete glucagon.
- In the liver...you should know what happens there.
- But lactate is brought into the liver to help out with pyruvate production.
- CO2 production seems to go way up.
- Glycerol and fatty acds are brought into the liver to prepare ketone bodies and glucose.
- Cortisol enters muscle.
43
Utterly Evil Question:
| What would we see in alcoholic fatty liver disease?
- Excess energy increase in NADH
| - Fatty acid synthesis DHAP (Glycerol) = Increased TAGs.
44
What is the process for alcohol processing?
- Starting with ethanol
- Enzyme Alcohol Dehydrogenase (Found in the Cytoplasm)
- NAD+ comes in, NADH and H+ leave
- Product is ... I think that's acetylaldehyde?
- Second Enzyme Acetylaldehyde Dehydrogenase (Found in the mitochondrial Matrix)
- NAD+ Comes In,
- NADH + H+ Comes out
- Final Product is Acetate.
- When there's high energy (Such as high ATP or High NAD+ or low NADH), DHAP becomes favored and is converted to glycerol 3 phosphate.
- Glycerol 3 phosphate produces triacylglycerols, aka fat.
45
Describe the SIR2 gene
- Deletion of a gene called SIR2 (silent information regulator 2) abolishes the ability of caloric restriction to lengthen life in yeast and roundworms So SIR2 seems to have something to do with longetivity.
- But we humans have something similar called SIRT1. Or Sirtuin 1.
- Sirtuins are NAD+ dependednt protein deacetylases.
- NAD+/NADH ration seems to control their activity
- Nicotinamide and NADH are inhibitors of the deacetylase reaction
- Oxidative metabolism, which drives conversion of NADH to NAD+ enhances sirtuin activity.
46
So what all does SIRT1 do?
Not totally sure, but
- Takes the mystery acetylated protein, NAD+ and deacetylates it.
- O-acetyl-ADP-ribose also leaves
- Product is nicotinamide.
47
Describe the NAMPT portion of lysine deacetylation
- Starting Product, Nicotinamide
- Enzyme Nicotinamide Phosphoribosyl Transferase
- 5 Phosphoribosyl Pyrophosphate (PRPP) Comes In,
- PPi Comes out.
- Product is NMN, or nicotinamide mononucleotide
- This is all part of a process known as salvage synthesis.
48
Describe NMNAT's job in salvage synthesis
- Starting product is NMN
- Enzyme NMNAT (NMN adenyl transferase)
- ATP Comes in
- PPi comes out
- Product is NAD.
49
What were the Penfield Studies
A memory research field where it was observed that amnesia patients had altered activity in their temporal lobe. Specifically around the hippocampus and amygdala.
50
Compare declarative memory to Procedural
Declarative Memory:
- Explicit memory of places, events, facts, and people
- Found in the temporal lobe
Procedural memory
- Implicit memory
- Perceptual motor learning and mental operations (Long-term...don't seem to pertain to amnesia, such as bike riding)
- Is not based in the temporal lobe. Not really sure where it happens, but maybe the striatum?
51
What are the two main memory receptors?
- NMDA receptors seem to receive low frequency receptions and release what looks like Calcium to activate CaM (calmodulin0
- AMPA seem more important and respond to high frequency stimulations and Calcium.
52
Describe learning and memory
Synaptic Reentry Reinforcement (SRR) occurs in the cerebral cortex. Memories form in the hippocampus. AMPA receptors are what fluctuates when a memory is "accessed". (Channels are tetrameric)
- It seems like AMPAs are able to be inserted and removed freely from the membrane, differing them from NMDA.
- Glutamate activates both types of receptors
- If enough coactivity is allowed, it expels magnesium into the channel, allowing sodium and calcium to rush in and potassium to rush out. Calcium strengthens the synapse.
- Biggest difference between this and GABA is that GABA uses Chloride, not calcium.
- Ultimate goal is to activate PKC
- So this is a glutamate ligand-gated calcium channel that activates PKC.
53
What are other forms of synaptic plasticity?
Long term depression (LTD) seems to be associated with NMDA-receptors and independent LTP
- NMDA induced by low frequency stimulation
- Can require NMDA activation and Ca2+/Calmodulin-dependent phosphatase vs. kinase.
- Can be NMDA independent via metabotrophic glutamate receptors (mGlur)
54
Compare the receptors again
- Magnesium seems to act as a "cork" on the receptor that can be popped off with sufficient amounts of glutamate.
- Only AMPA seems to bring in sodium since the NMDA is blocked by NDMA. Once sodium depolarizes the cell enough, it pops off the Mg.
- The now open NMDA accepts calcium (making it both a ligand and voltage gated channel. Calcium activates metabolic machinery
- Resulting in more AMPA receptors to be "constructed," allowing it to be easier accessed in the future.
55
So now that you have enough information to actually understand that one slide...wanna try again?
Low frequencies stimulations send moderate amounts of calcium into the NMDA channels. High frequencies send much more.
- Both are looking to activate the CaMKII or something...not totally sure.
- Hypothetically, increasing the number of NMDA receptors on a specimen can enhance their memory capability.
56
And once again, what is synaptic re-entry reinforcement?
- A candidate cellular process for consolidating and storing memory.
- May have a role in sleep
- Requires repeated NMDA and CaMKII signalling.
- Though I'm not 100% following, it seems that based on SRR, repetition "reinforcements" across increasingly long periods of time seem to decrease the required amount of stimulation to open.
57
Where does SRR occur?
In the cerebral cortex. However, "memories" form in the hypocampus.
- AMPA RECEPTORS ARE WHAT FLUCTUATE WHEN A MEMORY IS ACCESSED.
58
What is the general fate of proteins when digested
Degraded into Amino acids and oligopeptides in the lumen (which are further broken down in intestinal cells via peptidases)
59
What is ubiquitin's role in protein breakdown
ATP activates ubiquitin, bonding it to the E1 substrate. And then it...dies...somehow. Fuck.
60
What dictates a protein's lifetime?
The N-terminus Amino Acid. Some, like alanine, can last over 20 hours (half life). Others like Arg tend to destabilize in about 30 minutes.
61
What are the 3 big chaperone/modulators of protein maintenance?
- Proteasomes
- Autophagy
- ERAD
62
What are diseases that can result in misfolding?
Alzheimers, ALS, Sickle Cell Anemia, Parkinson's Disease, Cystic Fibrosis
- Sickle Cell is the most famous one, and is a point mutation that changes a Glutamate to a Valine in the Beta globulin chain of Hb. This exposes a hydrophobic patch that leads to polymerization. This causes reduced elasticity of red blood cells, causing extreme pain, tissue destruction, and anemia.
63
How do these chaperones cause diseases?
- Overactive degradation systems such as Autophagy and ERAD (Endoplasmic Reticulum Associated Degradation) cause accumulation of mutant misfolded or incomplete degraded proteins.
- The CFTR membrane channel is a good example, as an improperly folded CFTR can cause a deficiency in the channel leading to cystic fibrosis.
64
Describe improper localization
Can Occur when proteins are misfolded, such that they are not trafficked to their proper location
- Loss of function occurs in (for example) the destination because the protein never reached theere
- Gain of function may ultimately result as the mutant protein builds up in the liver causing damage.
65
Describe the Dominant Negative Mutation
A mutant protein antagonizes the function of the wild-type protein
- This causes loss of protein activity
- Examples include Epidemiolysis Bullosa Simplex, which affects Keratin Building
- Another example is any mutation in the p53 factor as mutations prevent it from interacting with MDM2 and are not able to activate protective gene pathways
66
Describe the gain-of-toxic function
- Protein conformational changes can cause dominant phenotypes
- Proteins become toxic
- Examples include:
- APOE4 disrupts mitochondrial function; impairs neurite outgrowth (alzheimers)
- (Cu/Zn) Superoxide Dismutase (SOD1)
- Src kiinases in cancer
67
Describe the amyloid accumulation
- Amyloid Fibers: Insoluble Protein aggregates
- Amyloidogenic proteinshave VQIVY sequence, and can cause amyloid-related diseases.
- Lower order oligomers cause toxic effect. Amyloid deposits could be a protective mechanism.
- Several amyloidogenic proteins form pore-like structures which disrupts the cell membrane integrity
- These are usually seen in elderly people as part of the natural agin process
- Individuals with mutations in the protein early in life.
- These are seen in cataracts (crystalins)
- Also associated with alzheimer's, parkinson's, amyloid lateral sclerosisspongiform encephalopathies, diabetes, and familial amyloidoses.
68
Describe the energy landscape of protein folding
Native state is thermodynamically preferred...but with misfolding, it goes even lower down into the amyloid fiber (least energy).
69
How do amyloids progress into plaque deposits?
First it gets seeded (nucleated into the intermediate), causing fibril formation, the fibril then deposits as plaque. not sure Why this deserved it's own question.
70
How do organisms maintain it's capacity to grow and reproduce?
Keystones include the DRA pathway (Detect, Respond, Adopt)
| - Intrinsic Induction of stress defense programs and resulting adaption can increase life expectancy
71
Describe Hormetic Stress
Applying moderate levels of stress could trigger beneficial and adaptive stress defense pathways, allowing longer life.
- Caloric restriction prolongs the lifespan (Yeast-Primates)
72
Describe protein turnover
It starts in the stomach with pepsin
- Terminates with the Proteasome.
- The catalytic 20S core contains active sites
- The regulatory 19S regulatory unit has a ubiquitin recycling mechanism.
- In other words, ubiquinated protein binds to the proteasome, which breaks it down into peptide fragments (releasing the ubiquitin) and ejecting the proteolyzed amino acid fragments.
These can do one of three things:
1. Left intact for further biosynthesis purposes
2. Broken down into carbon skeletons for glucose, glycogen, or fatty acid synthesis (or cell respiration)
3. Or disposed by the urea cycle
73
What is the urea formula
Glutamate's the key amino acid. (Nitrogen collector)
Sequesters amine groups from transamination/aminotransferase reactions.
- So first off, to prepare glutamate, alpha-amino acids have their nitrogen group transferred to an alpha-ketoglutarate using an aminotransferase enzyme. (giving us a glutamate and an alpha-keto acid).
- Next Glutamate is bonded to NAD+ + H2O using the enzyme, glutamate dehydrogenase. This results in an NADH, and an NH4+.
- Next (not totally sure how yet...) this goes through the Urea cycle to become Urea.
74
Let's try that again. Cuz you got plenty of time, right?
What's the first reaction of the urea formula
Step One: The Transamination Step
1. Alpha amino group is transferred to an alpha ketoacid. (Such as alpha Ketoglutarate?)
2. The reaction is coupled with ...i dunno.
3. Enzyme is called a amino transferase
4. Does what it says on the label: The amino group is simply switched with the amino group. I "think" this gives us a glutamate, but it's REALLY unclear on that.
75
Second step: to separating amino from amino acid
With the...I think...Glutamate product from before, i Think... reacts with glutamate dehydrogenase and NAD+ to give off a brief Schiff Base Intermediate, and NADH and H+.
- This intermediate takes a water and releases it's amino group. Ending product is conveniently the alpha keto glutarate that we used in that first step.
76
What are ALT and AST
First off, it should be established that Aspartate and Alpha-ketoglutarate have a reversible reaction with glutamate and oxaloacetate. Got that?
- ALT Stands for Alanine Aminotransferase (Which can reversibly convert pyruvate and glutamate into alanine and alphaketoglutarate.
- AST stands for Aspartate aminotransferase (Which can reversibly convert oxaloacetate and glutamate into aspartate and alpha-ketoglutarate.
- Both require the coenzyme pyridoxyl 5' phosphate (PLP)...a derivitive of Vitamin B6.
77
What happens to the nitrogen removed in muscle tissue?
NH4+ is toxic in the bloodstream, so I "think", or at least it "says" that it's removed as Gln and Ala in muscles.
- And by that I think it means the Glutamate cycle gets it to alanine, which can carry it into the liver where it's pulled off and attached to urea.
78
Describe the urea cycle (Best as you can in on description)
(These first two steps take place in the mitochondrial matrix of the liver cell)
1. Ammonia molecule joins with CO2 derivitive, HCO3- and uses two ATP to produce carbamoyl phosphate.
- Enzyme is rate-limiting carbamoyl phosphate synthetase
- Further Activated by (NAG)
2. Ornithine moves into the mitochondrial matrix and combines with the carbamoyl phosphate to form Citruline
- Enzyme Ornithine transcarbamoylase
(Steps 3 through 5 take place in the cytoplasm of the same liver cell)
3. Citriline leaves out the mitochondria into the CYTOSOL (starts with C) and combines with Aspartate and ATP to form Arginio-succinate
- Enzyme Argininosuccinate synthetase
4. Enzyme argininosuccinate lyase causes argininosuccinate to release Fumarate off of the end product, Arg
- Note that arginine supplies the second Amino group in urea
5. Enzyme Arginase hydrolyzes Arginine to release urea leaving it as it's original Ornithine. The ornithine travels back into the mitochondria to repeat the step
- this step can be inhibited by ornithine
- The urea is sent to the kidneys via blood for excretion.
79
Name the two exclusively ketogenic amino acids and what they're used for
Leucine, and Lysine. They're used to produce Acetyl CoA or Acetoacetate.
80
Name the 5 "mixed" amino acids that are both ketogenic and glucogenic.
- Isoleucine
- Tryptophan
- Phenylalanine
- Tyrosine
- Threonine
- The rest of them are exclusively Glucogenic amino acids and are used in pyruvate or TCA Cycle intermediates such as oxaloacetate, alphaketoglutarate, succinyl CoA, and fumarate.
81
Really? She's making us do this? Fine.
Name the 6 amino acids that become pyruvate
- Threonine (Can also be acetyl CoA, otherwise breaks down into Glycine)
- Tryptophan (Breaks down to Ala)
- Alanine
- Cysteine
- Glycine (Can also be used to help produce amino group, otherwise breaks down into Serine
- Serine.
82
Name the 4 amino acids that become Succinyl CoA
- Methionine
- Threonine
- Valine
- Isoleucine (Can also become Acetyl CoA
83
Name the ...1? Amino acid that can break down into acetyl CoA
Leucine is the main one.
- Can also become acetoacetate
- Apparently threonine and Isoleucine can..."help"? Not really sure
84
5 amino acids that help construct alpha keto glutarate
- Glutamine,
- Histidine,
- Arginine
- Proline
- All of which help create:
- Glutamate.
85
2 Amino Acids that becomes fumarate? (Should actually know this one already.)
...but you don't.
- Phenylalanine (breaks down into:)
- Tyrosine (Main ingredient. Can also be acetoacetate)
86
2 Key amino acids for oxaloacetate
- Aparagine (Breaks down into:)
| - Aspartate
87
When nitrogen leaves muscle, which amino acid must it be attached to?
Alanine
88
What does SDSL stand for?
Sight directed Spin Labeling. It's that usual bullshit. The protein has all of it's normal CYS residues identified.
Then it makes a mutant protein with 0-1 residues
This gets expressed and purified
Labeled with CYS specific spin label
6. Remove free label through SEC, Desalting, Diafiltration)
7. Assess Absence of free label
8. Check if mutated protein is functional, native structure is intact, and if biophysical properties retained.
- No, I don't get it either.
89
What can we do with SDSL
* Single CYS constructs
* Label with Fluorine for Fluorine NMR
* Used STD NMR (Stands for Saturation Transfer Difference)
* Label with MTSL for an EPR tag
* Fluorine protein is more important.
90
Describe the general structure of ELIC
The ELIC Ion channel conducts ions through it's pores. It's found in the membranes of neuron cells.
* Accepts neurotransmitters in the extracellular domain and anesthetics are received in the ennermembranous region. I think. Not positive on that one.
91
What are agonists?
The thing that's "supposed" to bind to a binding site. Allosteric modulatorrs can alter this by
- Changing the structure and closing the pore
- Transition the protein to a desensitized state
- Locking the protein into a non-conducting state.
92
Which Allosteric modification does ELIC undergo upon exposure to isogluorine
According to these notes, anesthetics can inhibit by just getting into the pore and physically blocking the passage.
Her research suggests that T189 is the Isofluorine's binding site.
