current research

Gallery

1bbo 2stw 2L9Y

1990-1995

144. Gronenborn, A.M., Nilges, M., Peanasky, R.J. & Clore, G.M.  Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinases inhibitors. Biochemistry 29, 183 (1990).

145. Forman-Kay, J.D., Gronenborn, A.M., Kay, L. E., Wingfield, P.T. & Clore, G.M. Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy. Biochemistry 29, 1566 (1990).

146. Gronenborn, A.M. & Clore, G.M.  Protein structure determination in solution by two-dimensional and three-dimensional nuclear magnetic resonance spectroscopy. Analytical Chemistry 62, 2 (1990).

147. Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T. & Gronenborn, A.M.  Complete resonance assignment for the polypeptide backbone of interleukin-1 using three-dimensional heteronuclear NMR spectroscopy. Biochemistry  29, 3542 (1990).

148. Driscoll, P.C., Gronenborn, A.M., Wingfield, P.T. & Clore, G.M.  Determination of the secondary structure and molecular topology of interleukin-1 using two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Biochemistry 29, 4668 (1990).

149. Clore, G.M., Appella, E., Yamada, M., Matsushima, K. & Gronenborn, A.M.  The three-dimensional structure of interleukin-8 in solution. Biochemistry 29, 1689 (1990).

150. Bax, A., Clore, G.M., Driscoll, P.C., Gronenborn, A.M., Ikura, M. & Kay, L.E.  Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins. J. Magn. Reson. 87, 620 (1990).

151. Bax, A., Clore, G.M. & Gronenborn, A.M. 1H-1H correlation via isotropic mixing of 13C magnetization: a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins. J. Magn. Reson. 88, 425 (1990).

152. Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C. & Gronenborn, A.M.  Deviations from the simple two parameter model free approach to the interpretation of 15N nuclear magnetic relaxation of proteins.  J. Am. Chem. Soc. 112, 5671 (1990).

153. Clore, G.M., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M.  Low resolution structure of interleukin-1 in solution derived from 1H-15N heteronuclear three-dimensional NMR spectroscopy.  J. Mol. Biol. 214, 811 (1990).

154. Clore, G.M., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M.  Analysis of backbone dynamics of interleukin-1 using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry 29, 7387 (1990).

155. Clore, G.M., Bax, A., Wingfield, P.T. & Gronenborn, A.M.  Identification and localization of bound internal water in the solution structure of interleukin-1 by heteronuclear three-dimensional 1H rotating frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy. Biochemistry 29, 4989 (1990).

156. Clore, G.M., Bax, A., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M.Assignment of the side chain 1H and 13C resonance of interleukin-1 using double and triple resonance heteronuclear three-dimensional NMR spectroscopy.  Biochemistry 29, 8172 (1990).

157. Kay, L.E., Clore, G.M., Bax, A. & Gronenborn, A.M.  Four-dimensional heteronuclear triple resonance NMR spectroscopy of interleukin-1in solution. Science 249, 411 (1990).

158. Clore, G.M. & Gronenborn, A.M.  Comparison of NMR and X-ray structures of hirudin. (1991).  In:   “Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy”, (ed. Hoch, J.C.), pp. 57-66, NATO ASI Series, Plenum Press, (1990).

159. Becerra, S.P., Clore, G.M., Gronenborn, A.M., Karlström, A., Stahl, S.J., Wilson, S.H. & Wingfield, P.T.  Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli. FEBS Lett. 270, 76 (1990).

160. Omichinski, J., Clore, G.M., Appella, E., Sakaguchi, K. & Gronenborn, A.M.  High resolution three-dimensional solution structure of a single zinc finger from a human enhancer binding protein in solution. Biochemistry 29, 9334 (1990).

161. Ikura, M., Bax, A., Clore, G.M. & Gronenborn, A.M.  Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy. J. Am. Chem. Soc. 112, 9020 (1990).

162. Clore, G.M., Kay, L.E., Bax, A. & Gronenborn, A.M.  Four dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin-1.  Biochemistry 30, 12 (1991).

163. Clore, G.M. & Gronenborn, A.M.  Two, three and four dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution. Ann. Rev. Biophys. Biophys. Chem. 20, 29 (1991),

164. Forman-Kay, J.D., Clore, G.M., Wingfield, P.T. & Gronenborn, A.M.  The high resolution three-dimensional structure of reduced recombinant human thioredoxin in solution.  Biochemistry 30, 2685 (1991).

165. Baldwin, E.T., Weber, I.T., St. Charles, R., Xuan, J.C., Appella, E., Yamada, M., Matsushima, K., Edwards, B.F.P., Clore, G.M., Gronenborn, A.M. & Wlodawer, A. Crystal structure of interleukin-8: symbiosis of NMR and crystallography. Proc. Natl. Acad. Sci. U.S.A. 88, 502 (1991).

166. Clore, G.M. & Gronenborn, A.M. Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8: possible implications for the mechanism of receptor binding. J. Mol. Biol. 217, 611 (1991).

167. Gronenborn, A.M. & Clore, G.M. Modeling the three-dimensional structure of the monocyte chemoattractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8. Protein Engineering 4, 263 (1991).

168. Clore, G.M., Bax, A. & Gronenborn, A.M.  Stereospecific assignment of -methylene protons in larger proteins using three-dimensional 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. J. Biomol. NMR 1, 13 (1991).

169. Clore, G.M., Wingfield, P.T. & Gronenborn, A.M.  High resolution three dimensional structure of interleukin-1 in solution by three and four dimensional nuclear magnetic resonance spectroscopy.  Biochemistry 30, 2315 (1991).

170. Clore, G.M. & Gronenborn, A.M.  NMR and X-ray analysis of the three-dimensional structure of interleukin-8.  In: “Neutrophil-Activating Peptides and other Chemotactic Cytokines”, (Baggiolini, M. & Sorg, C., eds.) 4, 18-40, S. Karger, Basel (1991).

171. Clore, G.M. & Gronenborn, A.M.  Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Progr. Nucl. Magn. Reson. Spectroscopy 23, 43 (1991).

172. Sakaguchi, K., Appella, E., Omichinski, J.G., Clore, G.M. & Gronenborn, A.M. Specific DNA binding to an MHC enhancer sequence by a synthetic 57-residue double zinc finger peptide from a human enhancer binding protein. J. Biol. Chem. 266, 7306 (1991).

173. Clore, G.M., Omichinski, J.G. & Gronenborn, A.M.  Slow conformational dynamics at the metal coordination site of a zinc finger. J. Am. Chem. Soc. 113, 4350 (1991).

174. Clore, G.M. & Gronenborn, A.M.  Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390 (1991).

175. Forman-Kay, J.D., Gronenborn, A.M., Wingfield, P.T. & Clore, G.M.  Determination of the positions of bound water in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol. 220, 209 (1991).

176. Clore, G.M. & Gronenborn, A.M.  Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1. J. Mol. Biol. 221, 47 (1991).

177. Powers, R., Gronenborn, A.M., Clore, G.M. & Bax, A. Three-dimensional triple resonance NMR of 13C/15N enriched proteins using constant-time evolution. J. Magn. Reson. 94, 209 (1991).

178. Gronenborn, A.M., Filpula, D.R., Essig, N.Z., Achari, A., Whitlow, M., Wingfield, P.T. & Clore, G.M. A novel highly stable fold of the immunoglobulin binding domain of Streptococcal protein G. Science 253, 657-661 (1991).

179. Powers, R., Clore, G.M., Bax, A., Garrett, D.S., Stahl, S.J., Wingfield, P.T. & Gronenborn, A.M.  Secondary structure of the ribonuclease H domain of the human immunodificiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. J. Mol. Biol. 221, 1081 (1991).

180. Garrett, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M.  A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214 (1991).

181. Omichinski J.G., Clore, G.M., Sakaguchi, K., Appella, E. & Gronenborn, A.M.  Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy. FEBS Lett. 292, 25 (1991).

182. Gronenborn, A.M. & Clore, G.M. Similarity of Protein G and Ubiquitin. Science 254, 581-582 (1991).

183. Clore, G.M. & Gronenborn, A.M.  Localization of bound water in the solution structure of the immunoglobulin binding domain of Streptococcal protein G: evidence for solvent induced helical distortions in solution.  J. Mol. Biol.223, 853 (1992).

184. Grzesiek, S., Ikura, M., Clore, G.M., Gronenborn, A.M. & Bax, A.  A 3D triple resonance NMR technique for qualitative measurement of carbonyl-H J couplings in isotopically enriched proteins. J. Magn. Reson. 96, 215 (1992).

185. Clore, G.M. & Gronenborn, A.M. Practical aspects of two, three and four-dimensional nuclear magnetic resonance spectroscopy applied to the study of protein structure.     In: Protein Engineering – a Practical Approach, (eds. Rees, A.R., Wetzel, R. & Sternberg, M.J.E.), Oxford University Press, pp. 33-52 (1992).

186. Omichinski, J.G., Clore, G.M., Robien, M., Sakaguchi, K., Appella, E. & Gronenborn, A.M.  High resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1.  Biochemistry 31, 3907 (1992).

187. Forman-Kay, J.D., Clore, G.M. & Gronenborn, A.M.  The relationship between electrostatics and redox function in human thioredoxin: charaterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.  Biochemistry 31, 3442 (1992).

188. Robien, M.A., Clore, G.M., Omichinski, J.G., Perham, R.N., Appella, E., Sakaguchi, K. & Gronenborn, A.M.  Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry 31, 3463 (1992).

189. Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M. & Clore, G.M. 1H, 15N, 13C and 13CO assignments of human interleukin-4 using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. Biochemistry 31, 4334 (1992).

190. Garrett, D.S., Powers, R., March, C.J., Frieden, E.A., Clore, G.M. & Gronenborn, A.M.  Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 31, 4347 (1992).

191. Chandrasasekhar, I., Clore, G.M., Szabo, A., Gronenborn, A.M. & Brooks, B.R. A 500 ps molecular dynamics simulation study of interleukin-1 in water: correlation with nuclear magnetic resonance spectroscopy and crystallography. J. Mol. Biol. 226, 239 (1992).

192. Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. & Bax, A. Solution structure of a calmodulin-target peptide complex by multi-dimensional NMR. Science 256, 632 (1992).

193. Powers, R., Garrett, D.S., March, C.J., Frieden. E.A., Gronenborn, A.M. & Clore, G.M. Three-dimensional solution structure of human interleukin-4 by multi-dimensional heteronuclear magnetic resonance spectroscopy. Science 256, 1673 (1992).

194. Forman-Kay, J.D., Clore, G.M., Stahl, S.J. & Gronenborn, A.M.  1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant.  J. Biomolec. NMR 2, 431 (1992).

195. Achari, A., Hale, S.P, Howard, A.J., Clore, G.M., Gronenborn, A.M., Hardman, K.D. & Whitlow, M.  The 1.67 Å X-ray structure of the B2 immunoglobulin domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry 31, 10449 (1992).

196. Shaanan, B., Gronenborn, A.M., Cohen, G.H., Gilliland, G.L., Veerapandian, B., Davies, D.R. & Clore, G.M.  Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement. Science 257, 961 (1992).

197. Rose, K., Simona, M.G., Savoy, L.A., Regamey, P.O., Green, B.N., Clore, G.M., Gronenborn, A.M. & Wingfield, P.T.  Pyruvic acid is attached through its central carbon atom to the amino terminus of the recombinant-DNA derived DNA-binding protein Ner of bacteriophage Mu. J. Biol. Chem. 267, 19101 (1992).

198. Powers, R., Clore, G.M., Stahl, S.J., Wingfield, P.T. & Gronenborn, A.M.  Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements. Biochemistry 31, 9150 (1992).

199. Omichinski, J.G., Trainor, C., Evans, T., Gronenborn, A.M., Clore, G.M. & Felsenfeld, G. A small single-‘finger’ peptide from the erythroid factor GATA-1 binds specifically to DNA as a zinc or iron complex. Proc. Natl. Acad. Sci. U.S.A. 90, 1676 (1993).

200. Grasberger, B.L., Gronenborn, A.M. & Clore, G.M. Analysis of the backbone dynamics of interleukin-8 by 15N relaxation measurements. J. Mol. Biol. 230, 364 (1993).

201. Clore, G.M., Robien, M.A. & Gronenborn, A.M.  Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 231, 82 (1993).

202. Vuister, G.W., Clore, G.M., Gronenborn, A.M., Powers, R., Garrett, D.S., Tschudin, R. & Bax, A. Increased resolution and improved spectral quality in four-dimensional 13C/13C separated HMQC-NOE-HMQC spectra using pulsed field gradients.  J. Magn. Reson. Series  B 101, 210 (1993).

203. Sakaguchi, K., Zambrano, N., Baldwin, E.T., Shapiro, B.A., Erickson, J.W., J.G. Omichinski, G.M. Clore, A.M. Gronenborn & Appella, E.  Identification of a binding site for the human immunodeficiency virus type I nucleocapsid protein. Proc. Natl. Acad. Sci. U.S.A. 90, 5219 (1993).

204. Varley, P., Gronenborn, A.M., Christensen, H., Wingfield, P.T., Pain, R.H. & Clore, G.M.   Kinetics of folding of the all -sheet protein interleukin-1 studied by nuclear magnetic resonance, circular dichroism and fluorescence. Science 240, 1110 (1993).

205. Powers, R., Clore, G.M., Garrett, D.S. & Gronenborn, A.M.  Relationships between the precision of high resolution protein NMR structures, solution order parameters and crystallographic B factors. J. Magn. Reson. Series B 101, 325-327 (1993).

206. Gronenborn, A.M. & Clore, G.M.  Structural studies of immunoglobulin binding domains of Streptococcal Protein G. ImmunoMethods 2, 3-8 (1993).

207. Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M. & Clore, G.M. The high resolution three-dimensional solution structure of human interleukin-4 determined by multi-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 32, 6744 (1993).

208. Gronenborn, A.M. & Clore, G.M. Identification of the contact surface of a Streptococcal protein G domain complexed with a human Fc fragment. J. Mol. Biol. 233, 331 (1993).

209. Clore, G.M. & Gronenborn, A.M. Structural studies of interleukin-1, interleukin-4 and interleukin-8 ImmunoMethods 3, 56-81 (1993).

210. Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R. & Nilges, M. Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261, 328 (1993).

211. Omichinski, J.G., Clore, G.M., Schaad, O., Felsenfeld, G., Trainor, C., Appella, E., Stahl, S.J. & Gronenborn, A.M.   NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science 261, 438-446 (1993).

212. Clore, G.M., Bax, A., Ikura, M. & Gronenborn, A.M. Structure of calmodulin-target peptide complexes. Current Opinion in Structural Biology. 3, 838-845 (1993).

213. Bax, A., Grzesiek, S., Gronenborn, A.M. & Clore, G.M. Isotope-filtered 2D HOHAHA spectroscopy of a peptide-protein complex using heteronuclear Hartmann-Hahn dephasing. J. Magn. Reson. 106 Series A, 269-273 (1994).

214. Gronenborn, A.M. & Clore, G.M. Experimental support for the “hydrophobic zipper” hypothesis of protein folding. Science 263, 536 (1994).

215. Barchi, J.J., Grasberger, B., Gronenborn, A.M. & Clore, G.M.  Investigation of the backbone dynamics of the IgG-binding domain of Streptococcal Protein G by heteronuclear two-dimensional 1H-15N nuclear magnetic resonance spectroscopy. Protein Science 3, 15-21 (1994).

216. Clore, G.M., Bax, A., Omichinski, J.G. & Gronenborn, A.M.  Localization of bound water in the solution structure of the specific complex of the erythroid transcription factor GATA-1 with DNA by water selective two-dimensional heteronuclear magnetic resonance spectroscopy. Structure 2, 89-94 (1994).

217. Clubb, R.T., Omichinski, J.G., Clore, G.M. & Gronenborn, A.M. Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type I human interleukin-8 receptor.    FEBS Lett.338, 93-97 (1994).

218. Garrett, D.S., Lodi, P.J., Shamoo, Y., Williams, K.R., Clore, G.M. & Gronenborn, A.M.  Determination of the secondary structure and folding topology of a RNA binding domain of the mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 33, 2852-2858 (1994).

219. Rozwarski, D.A., Gronenborn, A.M., Clore, G.M., Bazan, J.F., Bohm, A., Wlodawer, A., Hatada, M. & Karplus, P.A. Structural comparison among the short-chain helical cytokines. Structure 2, 159-173 (1994).

220. Lodi, P.J., Garrett, D.S., Kuszewski, J., Tsang, M.L.S., Weatherbee, J.A., Leonard, W.J., Gronenborn, A.M. & Clore, G.M.  High-resolution structure of the  chemokine hMIP-1 by multi-dimensional NMR.Science 263, 1762-1767 (1994).

221. Garrett, D.S., Kuszewski, J., Hancock, T.J., Lodi, P.J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M.  The impact of direct refinement against three-bond HN-CH coupling constants on protein structure determination by NMR. J. Magn. Reson. Series B 104, 99-103 (1994).

222. Gronenborn, A.M. & Clore, G.M.  Identification of N-terminal helix capping boxes by means of 13C chemical shifts. J. Biomol. NMR 4, 455-458 (1994).

223. Smith, L.J., Redfield, C., Smith, R.A.G., Dobson, C.M., Clore, G.M., Gronenborn, A.M., Walter, M.R., Naganbushan, T.L. & Wlodawer, A. Comparison of four independently determined structures of human recombinant interleukin-4. Nature Structural Biology 1, 301-310 (1994).

224. Werner, M.H., Clore, G.M., Gronenborn, A.M., Kondoh, A. & Fisher, R.J. Refolding proteins by gel filtration chromatography. FEBS Lett. 345, 125-130 (1994).

225. Qin, J., Clore, G.M. & Gronenborn, A.M.  The high resolution three-dimensional solution structure of the oxidized and reduced states of human thioredoxin: delineation of conformational differences between the two redox states. Structure 2, 503-522 (1994).

226. Werner, M.W., Clore, G.M., Gronenborn, A.M. & Nash, H.A.  Symmetry and asymmetry in the function of Escherichia coli integration host factor. Current Biology 4, 477-487 (1994).

227. Grasberger, B.L., Clore, G.M. & Gronenborn, A.M. High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH induced conformational transition in the reactive site. Structure 2, 669-678 (1994).

228. Makhatadze, G.I., Clore, G.M., Gronenborn, A.M. & Privalov, P.L.  Thermodynamics of unfolding of the all -sheet protein interleukin-1.  Biochemistry 33, 9327-9332 (1994).

229. Gronenborn, A.M. & Clore, G.M.  Where is NMR taking us?  Proteins: Struct. Funct. Genet. 19, 273-276 (1994).

230. Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E. & Gronenborn, A.M.  High-resolution solution structure of the oligomerization domain of p53 by multi-dimensional NMR. Science 265, 386-391 (1994).

231. Gronenborn, A.M. & Clore, G.M. Structural studies of interleukin-8 and interleukin-4. In: Structural Biology: The State of the Art. (Sarma, R.H. & Sarma, M.H., eds.) pp. 19-42, Adenine Press, New York (1994).

232. Wang, A.C., Lodi, P.J., Qin, J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. J. Magn. Reson. Series B 105, 196-198 (1994).

233. Covell, D.G., Smythers, G.W., Gronenborn, A.M. & Clore, G.M. Analysis of hydrophobicity in the  and  chemokine families and its relevance to dimerization. Protein Science 3, 2064-2072 (1994).

234. Kuszewski, J., Clore, G.M. & Gronenborn, A.M.  Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of Streptococcal Protein G. Protein Science 3, 1945-1952 (1994).

235. Clubb, R.T., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Gronenborn, A.M. & Clore, G.M.  A novel class of winged helix-turn-helix protein – the DNA binding domain of Mu transposase. Structure 2, 1041-1048 (1994).

236. Clore, G.M. & Gronenborn, A.M. Three-dimensional structures of  and  chemokines. FASEB Journal. 9, 57-62 (1995).

237. Kuszewski, J., Qin, J., Gronenborn, A.M. & Clore, G.M. The impact of direct refinement against 13C and 13C chemical shifts on protein structure determination by NMR. J. Magn. Reson.Series B 106, 92-96 (1995).

238. Ernst, J.A., Clubb, R.T., Zhou, H.-X., Gronenborn, A.M. & Clore, G.M.  Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science 267, 1813-1817 (1995).

239. Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E. & Gronenborn, A.M.  Interhelical angles in the solution structure of the oligomerization domain of the tumour suppressor p53. Science 267, 1515-1516 (1995).

240. Strzelecka, T.E., Hayes, J.J., Clore, G.M. & Gronenborn, A.M.  DNA binding specificity of the Mu Ner protein. Biochemistry 34, 2946-2955 (1995).

241. Qin, J., Clore, G.M., Kennedy, W.M.P., Huth, J.R. & Gronenborn, A.M.  Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFB.     Structure 3, 289-297 (1995).

242. Clore, G.M., Ernst, J., Clubb, R.T., Omichinski, J.G., Sakaguchi, K., Appella, E. & Gronenborn, A.M. Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nature Structural Biology 2, 321-332 (1995).

243. Clubb, R.T., Omichinski, J.G., Sakaguchi, K., Appella, E., Gronenborn, A.M. & Clore, G.M.   Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements. Protein Science 4, 855-862 (1995).

244. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. The impact of direct refinement against proton chemical shifts in protein structure determination by NMR. J. Magn. Reson. Series B 107, 293-297 (1995).

245. Werner, M.H., Huth, J.R., Gronenborn, A.M. & Clore, G.M.  Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex.  Cell 81, 705-714 (1995).

246. Balagurumoorthy, P., Sakamoto, K., Lewis, M.S., Zambrano, N., Clore, G.M., Gronenborn, A.M., Appella, E. & Harrington, R.E. Four p53 DNA binding domains bind natural p53 response elements and bend the DNA. Proc. Natl. Acad. Sci. U.S.A. 92, 8591-8595 (1995).

247. Lodi, P.J., Ernst, J.A., Kuszewski, J., Hickman, A.B., Engelman, A., Craigie, R., Clore, G.M. & Gronenborn, A.M.  Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry 34, 9826-9833. (1995).

248. Makhatadze, G.I., Clore, G.M. & Gronenborn, A.M.  Solvent isotope effect and protein stability. Nature Struct. Biol.2, 852-855 (1995).

249. Werner, M.H., Bianchi, M.E., Gronenborn, A.M. & Clore, G.M.  NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY. Biochemistry 34, 11998-12004 (1995).

250. Strzelecka, T.E., Clore, G.M. & Gronenborn, A.M.  The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif.  Structure 3, 1087-1095 (1995).

251. Gronenborn, A.M. & Clore, G.M. Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. Biol. 30, 351-385 (1995).