module 1.2 Flashcards
protein function, enzyme kinetics, enzyme regulation
what is the overal definition of hemoglobins structure in terms of polypeptide arrangement
dimer of two ab protomers
what is the fold of myoglobin and hemoglobin called?
globin fold
what is the immune protein containing 2 heavy chains, 2 light chains arranged in 12 domains of either FAB or constant classification called? what is the overall way of describing its polypeptide arrangement
immunoglobiulin g (iGg), dimer of 2 protomers
what is the repeating fold of iGg called? how many exist in a single iGg protein?
immunoglobulin-like fold, 12
what bonds stabilise iGg antibodies?
disulfide bonds
what is it called when a non-protein molecule integrates itself into a protein and becomes integral to its function? give example
prosthetic, heme group
what is the octahedral coordination complex central to a hemoglobin/myoglobin domain called? when is it planar and when isnt it planar?
heme group, planar in r state and non-planar in t state
why is the equilbrium dissociation constant preferred to the equilibrium association constant
M unit easier to work with than M^-1
what is the term given to the measure of a multi-species complexes tendancy to revert into its seperated forms
equilibrium dissociation constant
what is the abbreviation lettering of the equilibrium dissociation constant?
Kd
what is the abbreviation lettering of the equilibrium association constant?
Ka
what does the theta value refer to
the fraction of bound substates to the total amount of binding molecules (bound + not bound)
in a theta - ligand concentration curve, what is the asymptote approaching
the maximum theta value where all the binding molecules are occupied
how can the equilibrium dissociation constant be found by looking at a theta - ligand concentration graph?
finding the x axis value when the y axis is 0.5x theta max
what happens to a complexes tendency to dissociate as Kd increases
tendency to dissociate increases
