Chemistry Reference
In-Depth Information
br
ap
roader and b
pplied to a d
better under
drug discover
rstanding of
ry process.
f how NMR
R spectroscop
py techniqu
es can be
P
Protein-ligan
nd Binding A
Affinity and
d NMR Par
rameters
F
m
ca
of
dy
(R
E
irst of all, it
measure of ho
an be determ
f the bindin
ynamic equi
R), the free
Equation 1:
t is importan
ow strongly
mined from m
ng of small
ilibrium inv
ligand (L),
nt to bear in
that drug bin
measuremen
molecule lig
olved, wher
and the rece
mind that th
nds to the pr
nts of dissoci
gands and l
re three spec
eptor-ligand
he affinity of
rotein [17]. T
iation consta
large recepto
cies are pres
complex (R
f drug for pr
Then, bindin
ants (K
D
). In
or proteins
sent: the free
RL), as repre
rotein is a
ng affinity
n a system
there is a
e receptor
esented in
(1)
T
co
This equilibr
onstant (
k
off
)
rium has an
) (Scheme 1)
n association
) [7, 14, 18].
n rate consta
ant (
k
on
) an
nd a dissoci
ation rate
mplex (RL).
Sc
Sc
cheme 1:
NM
cheme adapted
MR properties
d from (Refs. [7
of receptor (
7, 14, 18]).
(R), ligands (L
L) and recept
tor-ligand com
F
eq
rom this, th
quilibrium d
he binding a
dissociation c
affinity can
constant (K
D
be quantifie
D
), given by
ed by the te
Equation 2 [
emperature-d
[17]:
dependent
(2)
