Nap Attack 6 Flashcards
Anfinsen’s dogma
at least for small globular proteins, tertiary structure is determined exclusively by primary structure (based on study of addition and removal of mercaptoethanol)
native structure represents
a unique, stable and kinetically accessible minimum of the free energy
chemical interactions that stabilize polypeptides
covalent bonds, disulfide bonds, salt bridges, hydrogen bonds, long-range electrostatic interactions, Van der Waals interactions
How is stabilization from these weak bonds possible
strength in numbers, many weak bonds can make a large stable structure
Advantages of stabilization through weak interactions
allow for dynamic interactions and permit energy and information to more about the cell (pulling apart dna)
biological covalent bond strengths
200-460 kJ/mol (stable but can be broken under physiological conditions)
biological weak interactions strength
0.4-30 kJ/mol (continuously broken and reformed)
disulfide bond fun facts
- proteins on the extracellular surface are no longer exposed to the reducing environment inside a cell
- non-reducing environment disulfide bonds can form between the side chains of cysteine residues
- found primarily in secreted extracellular proteins(eukaryotes)
- uncommon in prokaryotes
four primary types of non-covalent forces that promote and stabilize protein structure
- hydrogen bonds
- electrostatic interactions(Ionic)
- hydrophobic interactions
- van der waals interactions
Second law of thermodynamics
the total entropy (disorder) of a system and it’s surroundings always increases in a spontaneous process
when a non polar molecule is introduced into water
- a cavity is created
- displaced water molecules reposition to form hydrogen bonds because there are less ways of forming hydrogen bond
- decrease in entropy
- non polars collect to release water molecules
The presence of other molecules in aqueous solution
disrupts the hydrogen-binding of water
when water surrounds a hydrophobic molecule
- results in a highly structure shell, or solation layer, of water around the molecule (decreased entropy)
when non-polar groups cluster together
the extent of the solation layer decreases bc each group no presents its entire surface to the solution
- less energy required to encage clumps of molecules than individually
- favourable increase in entropy major thermodynamic driving force for association of hydrophobic groups in aqueous solutions
water is a
dynamic loose network of hydrogen bonds