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30 Cards in this Set
- Front
- Back
NONPOLAR Amino Acids (10)
|
GLY
ALA ---large,bulky,flexible LEU MET sulfur ILE VAL ----- flat, rigid, narrow aromatics TRP largest aromatic PHE smallest aromatic TYR polar-OH aromatic ---- PRO special imido ring |
|
POLAR charged (4)
|
basic
LYS weak base ARG weak base HIS VERY weak base imidazole acidic (std weak acids) GLU ASP |
|
POLAR uncharged (6*)
|
ASN-CHO addn
GLN-CHO addn CYS sulfur (in active sites,crosslinks) TYR aromatic with -OH SER--CHO addn on -OH THR |
|
hydrophobic shapes
|
smallest, no R group- GLY
aromatics( flat, rigid, narrow)- PHE (smallest),TRP (largest),TYR bends- PRO flexible,aliphatic, bulky: LEU,ILE,VAL,MET |
|
Stabilizing Protein Bonds (4)
|
1. disulfide convalent
2. charge-charge 3. H-bonds 4. hydrophobic Effect.... ---van der Waals and dispersion forces add up ---HYDROPHOBIC effect HUGE --- |
|
Gibb's Free Energy significance
|
ΔG=ΔH-TΔS.
ΔG -ve means SPONTANEOUS protein folding ΔS driven and WHOLE system is lower ΔG since increase in entropy |
|
Significance of Hydrophobic Effect
|
1.makes globular proteins globular
2.basis of cell membrane structure 3.key in dbl helix DNA |
|
Globular Protein Facts. Why are globular proteins globular?
|
1.hydrophobic R chains buried.
2.Polar, charged chains external for solubility AND 3.uncharged surface R groups are H bonded to water. TIGHTLY packed cluster inside away from H2O make them globular. |
|
PEPTIDE BONDS
|
rigid planar
loss of H2O btn NH2 and COOH |
|
describe protein folding in terms of entropy and enthalpy
|
1. protein orders :entropy lowers
2. hydrophobic effect : entropy of SYSTEM increase 3. heat given off when bonds are formed 4. heat taken up ALWAYS PART of HYDROPHOBIC effect during non-polar group removal from water. FFT: overall system ΔG=ΔH-TΔS is negative!!! |
|
Hydrophobic Effect: ΔG=ΔH-TΔS
|
system=protein and water
1. hydrophobic groups push water out and water squeezed to order and decrease entropy 2. HYDROPHOBIC EFFECT is response to +ΔS. Spontanous and rapid CLUSTERING and PACKING (VDW) of hydrophobic groups to increase ΔS of system (water has more degrees of freedom for motion) ALWAYS NET +ΔS and NET +ΔH.ENTROPY DRIVEN |
|
inherited disease causes and examples
|
folding errors: sickle cell anemia.
one mutation in Hb causes tetramer aggregates and insolubility. RBC changes shape, and becomes inflexible causing anoxia. pain. cell death. |
|
Law of Mass Action relating to 1.Keq and 2.H/H eqn
|
law of mass action applies to ANY equilibrium:
ratio of conc of prod to reatant is always at constant when at equilibrium. H/H takes applies to all weak acids/weak bases and related pKa and pH. Form of Law of Mass action. |
|
IMPORTANT pKa's:
HIS, ASP,GLU, LYS,ARG |
HIS. pKa = 6.5
ARG,LYS = >10 GLU,ASP = <4.5 |
|
****determining proteins acidity or basicity****
|
asp+glu...acidic
arg+lys...basic |
|
NONPOLAR Amino Acids (10)
|
GLY
ALA ---large,bulky,flexible LEU MET sulfur ILE VAL ----- flat, rigid, narrow aromatics TRP largest aromatic PHE smallest aromatic TYR polar-OH aromatic ---- PRO special imido ring |
|
POLAR charged (4)
|
basic
LYS weak base ARG weak base HIS VERY weak base imidazole acidic (std weak acids) GLU ASP |
|
POLAR uncharged (6*)
|
ASN-CHO addn
GLN-CHO addn CYS sulfur (in active sites,crosslinks) TYR aromatic with -OH SER--CHO addn on -OH THR |
|
hydrophobic shapes
|
smallest, no R group- GLY
aromatics( flat, rigid, narrow)- PHE (smallest),TRP (largest),TYR bends- PRO flexible,aliphatic, bulky: LEU,ILE,VAL,MET |
|
Stabilizing Protein Bonds (4)
|
1. disulfide convalent
2. charge-charge 3. H-bonds 4. hydrophobic Effect.... ---van der Waals and dispersion forces add up ---HYDROPHOBIC effect HUGE --- |
|
Gibb's Free Energy significance
|
ΔG=ΔH-TΔS.
ΔG -ve means SPONTANEOUS protein folding ΔS driven and WHOLE system is lower ΔG since increase in entropy |
|
Significance of Hydrophobic Effect
|
1.makes globular proteins globular
2.basis of cell membrane structure 3.key in dbl helix DNA |
|
Globular Protein Facts. Why are globular proteins globular?
|
1.hydrophobic R chains buried.
2.Polar, charged chains external for solubility AND 3.uncharged surface R groups are H bonded to water. TIGHTLY packed cluster inside away from H2O make them globular. |
|
PEPTIDE BONDS
|
rigid planar
loss of H2O btn NH2 and COOH |
|
describe protein folding in terms of entropy and enthalpy
|
1. protein orders :entropy lowers
2. hydrophobic effect : entropy of SYSTEM increase 3. heat given off when bonds are formed 4. heat taken up ALWAYS PART of HYDROPHOBIC effect during non-polar group removal from water. FFT: overall system ΔG=ΔH-TΔS is negative!!! |
|
Hydrophobic Effect: ΔG=ΔH-TΔS
|
system=protein and water
1. hydrophobic groups push water out and water squeezed to order and decrease entropy 2. HYDROPHOBIC EFFECT is response to +ΔS. Spontanous and rapid CLUSTERING and PACKING (VDW) of hydrophobic groups to increase ΔS of system (water has more degrees of freedom for motion) ALWAYS NET +ΔS and NET +ΔH.ENTROPY DRIVEN |
|
inherited disease causes and examples
|
folding errors: sickle cell anemia.
one mutation in Hb causes tetramer aggregates and insolubility. RBC changes shape, and becomes inflexible causing anoxia. pain. cell death. |
|
Law of Mass Action relating to 1.Keq and 2.H/H eqn
|
law of mass action applies to ANY equilibrium:
ratio of conc of prod to reatant is always at constant when at equilibrium. H/H takes applies to all weak acids/weak bases and related pKa and pH. Form of Law of Mass action. |
|
IMPORTANT pKa's:
HIS, ASP,GLU, LYS,ARG |
HIS. pKa = 6.5
ARG,LYS = >10 GLU,ASP = <4.5 |
|
****determining proteins acidity or basicity****
|
asp+glu...acidic
arg+lys...basic |