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30 Cards in this Set

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  • 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