Points To Remember Exam 1 Flashcards
What happens to Heat transfer when Change in entropy goes up
It goes up
What happens to Change in Entropy when Temperature goes up
It goes down because it is harder to release heat to heat
What Bonds are the most strong
Covalent
What Does A Low Pka tell us about the acidity
it is very acidic
What Amino Acids Absorb Wavelength and at What Wavelength
Tyrosine and Tryptophan absorb at 280
What does adding an acidic or basic Amino acid do to PI
Adding an Acidic Amino acid like Asp - will decrease the pI (net neutral is at a lower pH)
Adding a Basic Amino acid will increase the pI
Benzocaine Effects
ADA says that it can lead to Methemoglobin in Teething Toddler meaning it will go from ferrous to ferric and bind water instead of Oxygen
Where is myoglobin found
Red Muscle
Why does the Myoglobin not have a bohr effect or bind things allosterically
it only has two histidines and none of the Asp His interaction. it is not allosterically affect it is a hyperbollic curve
What is the prosthetic group of the hemoglobin
ferroprotoporphryin
Does Hemoglobin Act Sequentially or Concertadly
Sequentially
What Stabalizes the Hemoglobin T state
Salt Bridges
BPGs relation to Fetal Hemoglobin
Normally BPG stabalizes T state moving hemoglobin right (it is highly negative and binds to the positive hemoglobin)
Infants have serines not histidine so the BPG does not bind
Mechanism of the Bohr Effect (2 ways)
Decrease in pH protonates His146 and this will interact with the Asp 94 and thus pull F8 and the iron out of the plane thus releasing oxygen
the other way is that CO2 binds the amino end of hemoglobing making carbamino hemoglobin and stabalizing salt bridges
What Wavelengths show Oxyhemoglobin and Deoxyhemoglobin
940nm - Oxyhemoglobin
660nm- Deoxyhemoglobin
Magnetism and Oxygenated vs Deoxygenated
deoxygenated is magnetic (paramagnetic)
oxygenated is nonmagnetic (diamagnatic)
Glucose affect on hemoglobin
diabetes causes HbA1C which is glycosylated hemoglobin.
The Schiff Base happens on to hemoglobin which is reversible
but the amidori reaction is irreversible
Mutation in Sickle Cell
GTG -> GAG so Glu becomes Val
The affect Sickle cell has on pI
Sickle Cell has more net positive below pI and less negative above the pI than normal
Alpha and Beta Thalassemia
Alpha is missing Alpha only has Beta subunits of hemoglobin so it binds oxygen with no cooperative
Beta is missing Beta and only Alpha
loses oxygen binding and cooperativity
Cofactors Vs Coenzymes
Cofactors are small and inorganic and coenzymes are large organic
What Cofactors does Kinase Need
Mg to stabilize and Calcium concentration depended
Trypsin
Cleaves Basic Amino acids arginine and lysine
Chymotrypsin
Cleaves large hydrophobic aoromatic at the carboxyl side.
Like Phe Met Trp Tyr
Thrombin
cleaves at Arg-gly bonds
Elastase
cleaves small uncharged side chains. Like Valine
it is a serine protease in pancrease to remove elastin and is released in pancreas
is seen a degrader of elastin in the mouth
Is water in the active site
no
What are the Michaelis Menton Assumptions (3)
Formation and breakdown are at a steady state
Product formation is irreversible (k4 =0)
K2 is way less than K3
Km formula
Km = K2 +K3/K1
V formation Equation
K1[s][E]
VBreakdown Equation
(K2+K3)[ES]
What is the Michaelis Menton Equation
V= Vmax[S]/(Km+[S])
What is Kcat
K3
Reading the lineweaver Burke Plot
X Axis = 1/S
Y Axis 1/V
X Intercept = -1/km
Y Intercept = 1/Vmax
Malonate Succinate Inhibition Example
Malonate looks like succinate so it is competitive inhibition
DIPF/DFP
Di-isopropyl Fluorophophate - an inactivator of serine proteases by covalent interaction, and it is not reversible
Where do Allosterically affected enyzmes act in cell pathways
they usually act on the rate limiting or committed steps
Concerted Allosteric Model
When one substrate binds to the enzyme the whole thing will open up in to the R state