Biochem week 2 Flashcards
histidine
protonated state of histidine has a positive charge, deprotonated state has a neutral charge
glucagon
hormone that regulates glycolysis
beta turn (secondary protein structure)
H-bonds between carbonyl-O of first residue and the amide-H of the fourth residue
Thermodynamics of protein folding
conformational entropy is large
entropy of protein decreases
free energy of protein decreases
native structure has the lowest free energy (delta G)
overall entropy of H20 increases
Amyloidoses
while a protein is folding, sometimes multiple proteins that are folding, their intermediates (molten globular state) can interact with each other and form an amyloid structure
These self associated proteins aggregate -> cause diseases
cofactors
anything that will bind to a protein and affect protein structure
prosthetic groups
cofactors that bind irreversibly to proteins
substrate
cofactors that bind reversibly to proteins
Beer lambert law
Abs=ACL
A= extinction coefficient C= concentration L= length of light path
s-adenosyl methionine
methyl group donor for most biological methylation
Inorganic elements as cofactors
serve to maintain active conformations and as electron carrier
coenzyme A
carrier of acyl groups
business end is a sulfhydryl group which forms a thioester bond with organic acids
used for biosynthetic rxns (trigylcerides and fatty acid containing lipids)
Why do lipids associate in water?
As the lipids aggregate in water, there is an increase in disorder of water molecules therefore the entropy increases and the delta G decreases. The overall system is favorable
deltaG = deltaH - TdeltaS