Skildum/ Prunuske Week 1 Flashcards
(53 cards)
Which are the nonpolar, aliphatic amino acids?
Glycine (G, R= H) Alanine (A, R= CH3) Proline (P, R= ring structure) Valine (V, R= CH with 2 CH3 groups) Leucine (L, R= CH2-CH with 2 CH3 groups) Isoleucine (I, R= C bound to a CH3 and CH2-CH3)
Which are the aromatic amino acids?
Phenylalanine (F, R= Ch2-benzene)
Tyrosine (Y, R= CH2- benzene with para OH)
Tryptophan (W, R= big structure with 2 rings)
Which are the polar, uncharged amino acids?
Asparagine (N, R= CH2- C=O-NH2)
Glutamine (Q, R= CH2-CH2-C=O-NH2)
Serine (S, R=CH2OH)
Threonine (T, R= CH bonded to OH and CH3)
Which are the sulfur containing amino acids?
Methionine (M, R= CH2-CH2-S-CH3)
Cysteine (C, R= CH2-SH)
Which are the negatively charged (acidic) amino acids?
Aspartate (D, R= CH2, COO-)
Glutamate (E, R= CH2-CH2-COO-)
Which are the positively charged (basic) amino acids?
Arginine (R, R= CH2-CH2-CH2-NH-C=NH2+ and NH2 on last carbon
Lysine (K, R= CH2-CH2-CH2-CH2-NH3+)
Histidine (H, R= CH2- ring structure)
What is a peptide bond and how is it formed?
bond in amino acids between carbonyl carbon and nitrogen
-formed through dehydration reaction (releases H2O)
What are the 2 main structures in secondary proteins?
Alpha helix- R groups stick on outside
beta sheets- R groups stick up and down
What is Creutzfeldt Jakob’s disease caused by?
prion disease, increases in protein beta sheets which leads to amyloid fibers
Normal = PrP^c
Abnormal = PrP^sc
Where does ubiquitin tag bring misfolded proteins?
To the proteasome to be destroyed
What are the components of hemoglobin?
2 beta and 2 alpha subunits
Cooperatively binds oxygen (sigmoidal curve)
What are hemoglobin T and R states?
T state- promoted by 2,3-BPG (allosteric modulator) promotes O2 dissociation
R state- relaxed, easier for O2 to bind
What is the blood test to test for diabetes? (glycosylation on hemoglobin)
HbA1C
The base pair mutation of what to what amino acid causes sickle cell anemia?
From glutamate (negatively charge) to valine (nonpolar) on position 6 of beta subunit
What do these problems with Hb mean? HbS HbSS HbAA HbSA HbC
HbS- glu6val, sickle cell HbSS- alpha 2 beta 2^s- sickle cell HbAA- alpha2 beta 2^a normal HbSA- sickle cell trait HbC- Glu6Lysine -lysine in the spot of glutamate
What is thalassemia?
altered ratio of alpha beta hemoglobin, usually 1 is not produced
What is deltaS in the Gibbs free energy equation and what does increase or decrease mean?
Entropy.
deltaS > 0 is order decreasing (more randomness)
deltaS < 0 is order increasing (less randomness)
What does it mean if the Michaelis-Menten constant (Km) decreases?:
Takes less concentration for enzyme to reach Vmax so:
The enzyme is more active
What is a competitive inhibitor and does Km or Vmax change?
It competes at substrate binding sites
-increases Km but does not change Vmax
What is a noncompetitive inhibitor and does Km or Vmax change?
Molecules which bind an enzyme and inhibit its activity without inhibiting substrate binding (ex: suicide inhibitors)
-decreases Vmax but does not change Km
What is an allosteric inhibitor?
a molecule that binds an enzyme away from active substrate binding site and causes conformational change to prevent substrate binding
- cannot be described by Michaelis- Menten
- hyperbolic to sigmoidal curve)
Why do people with sickle cell have jaundice?
Sickle red blood cells turnover faster than normal RBCs
-heme breaks down into bilirubin and liver is overwhelmed–> causes discoloration
What are treatments for sickle cell?
only cure is a bone marrow transplant
- Hydroxyurea- drug that increases production of fetal (gamma) Hb subunits
- blood transfulsion
What are the oxidation/ reduction cofactors?
NADH, NADPH, PAD, metals, ascorbic acid
