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NMR spectroscopy in structure-based drug design Roberts 45 Gardner KH: Solution NMR spectroscopy beyond 25 kDa striction of loop motions upon binding inositol trisphosphate pin Struct Bio/ 1997, 7: 722-731 J Mol Biol1998,280:8798s 12. Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM: Defining nination from the ected diffusion anisotropy. Nat Struct Bio/ 1997, 4: 443-449 be obtained from simple (T1 T2 and NOE)relaxation measurements. Tjandra N, Bax A: Direct measurement of distances and angles in nolecules by Nmr in a dilute liquid crystalline medium. 6. Olejniczak ET, zhou M-M, Fesik SW: Changes in the NMR-derived 997278:1111-1114 is an important addition to the available methods for obtaining structural are motionally restricted in the free protein; others become more restricted information from Nmr on peptide binding -including some residues that do not contact the ligand 14. Peruvshkin K, Riek R, Wider G, Wuthrich K: Att 27. Wittekind M, Mapelli Lee V, Goldfarb V, Friedrichs MS, Meyers CA, The in shtinsmemt gans g2 267-g38o5ings and H and t-C chemical netic field leads to differing linewidths for the components of The NmR structure of this peptide-SH3 domain complex shows that the to extend substantially the upper size limit for studying proteins by nm ity of fluctuating hydrogen bonding interactions is discussed in which a protein can interact with alternative acceptors on the Palmer AG Il; Probing molecular motion by NMR. Curr Opin Struct 28. Kay LE, Muhandir Wolf G, Shoelson SE, Forman- Kay JD studying internal motion in proteins. 8:io 1998. at sH2 domain 16. Jardetzky O: Protein d allosteric proteins. Prog Brophys Mol Bio/ 1996, 65: 171-218 L, Hilbers Cw, Nilges M: Esser le discussion of the rela- y NMR structure ensembl tionships between dynamics, binding thermodynamics and specificity S Whitman CP: 15N NMR of the structural ensembles obtained by nmr amics and entropy changes of an kke M, Bruschweiler R, Palmer AG ll: NMR order parameters and criterion for inclusion of structures in the NMI Ca2+ binding by calbindin D9k. J Am Chem Soc 1993 ensemble to ensure that amplitudes of motion are better represented vector fluctuations measured from NMR- derived order ibronectin type lll domain. Nat Struct Bio/ 1998, 5: 55 59 protein folding. J Mol Bio/ 1996 Nieto PM, Birdsall B, Morgan WD, Frenkiel TA, Gargaro AR, Feeney 3: 32. Feeney J: NMR studies of interactions of ligands with dihydrofolate reductase, Biochem Pharmaco/ 0:141-152 and carboxylate groups in protein ligand complexes. FEBS Le 997,405:1620 eductase and their Design. Edited by Craik D. New York mation of unligated human cyclophilin A. J Mol Bio/ 1997 2726481 34. Birdsall B, Casarotto MG, Cheung AHT, Basran J, Roberts GCK 21. Hodson ME Discrete backbone disorder in the nuclear feeley j: The influence of aspartate 26 on the tautomeric forms of tobacillus casei dihydrofolate reductase. FEBS the mechanism of ligand entry. An illustration of the value of NMR in identifying 97.36:1450-1460 of folate and NADP+ with th See annotation to 22 22. Hodson ME Cistola, DF Iters the backbone conformations g protein as monitored by of the complex, and selectively [3C-Aspl-labelled enzyme was used to study veste aspartIc 35. Ross A, Slazmann M, Senn H: Fast-HMQc using Ernst angle acid binding protein and the way in proteins. J Biomol NMR 389396. required for access of the fatty acid 36. Tilley JW, Chen L, Fry DC on SD, Powers GD, Biondi D. tification of a 3. Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamil which binds to IL-2. J Am Chem Soc 1997,119: 7589-7590 See annotation to[22·」 bor TM, Feng S, Shirai F, Schre ased selection 266:173-194. 38. Farmer B Goldfarb V, Friedrichs MS, Wittekind M 25. Gryk MR, Abseher R, Simon B, Nilges M, Oschkinat H e MurB enzyme by nmR. Nat Struct Bio! 1996 Heteronuclear relaxation study of the Ph domain of B-spectrin 3:995997
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