Chemistry Reference
In-Depth Information
[96] Mayer, M. and Meyer, B., Group epitope mapping by saturation transfer difference NMR to
identify segments of a ligand in direct contact with a protein receptor.
J Am Chem Soc
, 2001,
123
, 6108-6117.
[97] Sandstrom, C.,
et al
., Atomic mapping of the interactions between the antiviral agent
cyanovirin-N and oligomannosides by saturation-transfer difference NMR.
Biochemistry
,
2004,
43
, 13926-13931.
[98] Hajduk, P. J.,
et al
., SOS-NMR: a saturation transfer NMR-based method for determ-
ining the structures of protein-ligand complexes.
J Am Chem Soc
, 2004,
126
,
2390-2398.
[99] Benie, A. J.,
et al
., Virus-ligand interactions: identification and characterization of ligand
binding by NMR spectroscopy.
J Am Chem Soc
, 2003,
125
, 14-15.
[100] Meinecke, R. and Meyer, B., Determination of the binding specificity of an integral mem-
brane protein by saturation transfer difference NMR: RGD peptide ligands binding to integrin
alphaIIbbeta3.
J Med Chem
, 2001,
44
, 3059-3065.
[101] Claasen, B.,
et al
., Direct observation of ligand binding tomembrane proteins in living cells by a
saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly
higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes.
J Am Chem
Soc
, 2005,
127
, 916-919.
[102] Dalvit, C., Homonuclear 1D and 2D NMR experiments for the observation of solvent-solute
interactions.
J Magn Reson B
, 1996,
112
, 282-288.
[103] Johnson, E. C.,
et al
., Application of NMR SHAPES screening to an RNA target.
J Am Chem
Soc
, 2003,
125
, 15724-15725.
[104] Di Micco, S.,
et al
., Differential-frequency saturation transfer difference NMR spectroscopy
allows the detection of different ligand-DNA binding modes.
Angew Chem Int Ed
, 2006,
45
,
224-228.
[105] Feeney, J.,
et al
., The effects of intermediate exchange processes on the estimation of
equilibrium constants by NMR.
J Magn Reson
1979,
33
, 519-529.
[106] Meiboom, S. and Gill, D., Modified spin-echo method for measuring nuclear relaxation times.
Rev. Sci. Instrum
., 1958,
29
, 688-691.
[107] van Dongen, M.,
et al
., Structure-based screening and design in drug discovery.
Drug Discov
Today
, 2002,
7
, 471-478.
[108] Hajduk, P. J.,
et al
., NMR-based screening of proteins containing
13
C-labeled methyl groups.
J Am Chem Soc
, 2000,
122
, 7898-7904.
[109] Weigelt, J.,
et al
., Site-selective screening by NMR spectroscopy with labeled amino acid pairs.
J Am Chem Soc
, 2002,
124
, 2446-2447.
[110] Weigelt, J.,
et al
., Site-selective labeling strategies for screening by NMR.
Comb Chem High
Throughput Screen
, 2002,
5
, 623-630.
[111] McCoy, M.A. andWyss, D. F., Spatial localization of ligand binding sites from electron current
density surfaces calculated from NMR chemical shift perturbations.
J Am Chem Soc
, 2002,
124
, 11758-11763.
[112] McCoy, M. A.,
et al
., Screening of protein kinases by ATP-STD NMR spectroscopy.
JAm
Chem Soc
, 2005,
127
, 7978-7979.
[113] Cheng,Y. and Prusoff,W. H., Relationship between the inhibition constant (
K
1
) and the concen-
tration of inhibitor which causes 50 per cent inhibition (
I
50
) of an enzymatic reaction.
Biochem
Pharmacol
, 1973,
22
, 3099-3108.
[114] Sanchez-Pedregal, V. M.,
et al
., The INPHARMAmethod: protein-mediated interligand NOEs
for pharmacophore mapping.
Angew Chem Int Ed
, 2005,
44
, 4172-4175.
[115] Banaszak, L.,
et al
., Lipid-binding proteins: a family of fatty acid and retinoid transport
proteins.
Adv Protein Chem
, 1994,
45
, 89-151.