NMR spectroscopy in structure-based drug design Roberts 47 69. LaPlante SR iizachew D. Moffett DB, Bus Wester WM. Dratz EA e conformation of the CD4 36-59 Transferred NOE experiments, including identification of spin diffusion mali F Do a-T. Doan B-T A, Palmas P. Sk te MR and MD study Proteins crystal structures of CD4, suggesting a change in conformation on binding Two peptide inhibitors of factor Xa, obtained by library screening, were stud. 73. Benitez BAS. ith EGF-like domain of thrombomodulin an EGF-like domai isolation and in the binding site (see also [58]), systematica d ng possible orientation of the 273:913-926. otained, suggesting that the inhibitors bind differently from the substrate, The structure of a loop in this domain which forms part of its thrombi made it possible to explain the specificity of the inhibitors. 71 but clearty not identical. This and the on from the Nmr structure of preceding paper [72] show the value of transferred NOE experiments in band 3 peptide inhibitor bound to glyceraldehyde-3phosphate g access to the peptide conformation in the bound state, as a me dehydrogenase. Biochemistry 1998, 37: 867-877 tic drugs