CHAPTER 2 - PROTEIN STRUCTURE
F: THERMODYNAMICS AND IMFs IN PROTEIN STABILITY
BIOCHEMISTRY - DR. JAKUBOWSKI
Last Update:
3/2/16
Learning Goals/Objectives for Chapter 2F: After class and
this reading, students will be able to ...
- Differentiate between general charge and specific ion-ion
pairs and summarize their role in protein stability
- Draw the structure of N-methylacetamide (NMA) and explain
why it is a useful small molecule model to study the role of H
bonds in protein stability
- Draw a thermodynamics cycle for the transfer of a hydrogen
bonded dimer of NMA from water to a nonpolar environment. From
the DG0 for steps in the cycle, and extending this model to
protein, predict if buried H bond formation drives protein
folding
- Explain if studies of low temperature protein denaturation,
high temperature protein, and DGo transfer of nonpolar side
chains from water to more nonpolar solvents support the
hydrophobic effect in protein stability
- summarize the relationship between the empirical Hofmeister
series and preferential binding of reagents into the hydration
sphere of protein to explain the effects of denaturants (urea,
guanidine salts) and stabilizers (glycerol, ammonium sulfate) on
proteins
-
Using benzene solubility in water as a model to study the
role of hydrophobic effect in protein unfolding and by inference
in protein stability, interpret graphs of DG0, DH0, DS0 and DCp
for the transfer of benzene to water, as a function of
temperature.
-
from the above graph, explain if trends in the thermodynamic
parameters for benzene transfer into water predict the observed
protein unfolding/stability behavior of proteins as a function
of temperature?
-
Give a molecular interpretation of the observed DCp for the
transfer of nonpolar molecules into water.
-
Describe chain conformational entropy, relate it to
conformational changes in acyl side chains in single and double
chain amphiphiles with temperatures, and describe it role in
protein stability.
-
state which of several given explanations for the observed
destabilizing effects of Asn to Ala mutations in protein account
for those observation
-
summarize graphically the magnitude and direction of the
major contributors (inter- and intramolecular forces and
effects) to protein stability
|
F1.
Introduction to Protein Stability
F2.
Ion - Ion Interactions
F3.
Hydrogen Bonding
F4.
Hydrophobic Interactions: Introduction
F5.
Additives and Their Interactions with Protein Surfaces
F6.
The Hydrophobic Effect and Change in Heat Capacity
F7.
Hydrophobic Effect and Protein Denaturation
F8. Mutagenesis and Protein Stability
F9.
Protein Stability and Molecular Orbitals
F10. Protein Stability in Thermophilic Organisms
F11.
General Links and References
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Chapter 2F: Thermodynamics and IMFs of Protein Stability
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