-
2
-
-
0020475314
-
Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution nuclear magnetic resonance
-
Wüthrich K., Wider G., Wagner G., Braun W. Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution nuclear magnetic resonance. J. Mol. Biol. 155:1982;311-319.
-
(1982)
J. Mol. Biol.
, vol.155
, pp. 311-319
-
-
Wüthrich, K.1
Wider, G.2
Wagner, G.3
Braun, W.4
-
3
-
-
0019327003
-
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
-
Kumar A., Ernst R.R., Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
-
(1980)
Biochem. Biophys. Res. Commun.
, vol.95
, pp. 1-6
-
-
Kumar, A.1
Ernst, R.R.2
Wüthrich, K.3
-
6
-
-
0024997404
-
Protein-DNA contacts in the structure of a homeodomian-DNA complex determined by nuclear magnetic resonance spectroscopy in solution
-
Otting G., Qian Y.Q., Billeter M., Muller M., Affolter M., Gehring W.J., Wüthrich K. Protein-DNA contacts in the structure of a homeodomian-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9:1990;3085-3092.
-
(1990)
EMBO J.
, vol.9
, pp. 3085-3092
-
-
Otting, G.1
Qian, Y.Q.2
Billeter, M.3
Muller, M.4
Affolter, M.5
Gehring, W.J.6
Wüthrich, K.7
-
7
-
-
0028473782
-
Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex
-
Spitzfaden C., Braun W., Wider G., Widmer H., Wüthrich K. Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex. J. Biomol. NMR. 4:1994;463-482.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 463-482
-
-
Spitzfaden, C.1
Braun, W.2
Wider, G.3
Widmer, H.4
Wüthrich, K.5
-
8
-
-
0029937271
-
NMR structure of the mouse prion protein domain PrP(121-231)
-
Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature. 382:1996;180-182.
-
(1996)
Nature
, vol.382
, pp. 180-182
-
-
Riek, R.1
Hornemann, S.2
Wider, G.3
Billeter, M.4
Glockshuber, R.5
Wüthrich, K.6
-
9
-
-
0035956956
-
Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
-
Fernandez C., Adeishvili K., Wüthrich K. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA. 98:2001;2358-2363.
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 2358-2363
-
-
Fernandez, C.1
Adeishvili, K.2
Wüthrich, K.3
-
10
-
-
0016433835
-
NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor
-
Wüthrich K., Wagner G. NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor. FEBS Lett. 50:1975;265-268.
-
(1975)
FEBS Lett.
, vol.50
, pp. 265-268
-
-
Wüthrich, K.1
Wagner, G.2
-
11
-
-
0022399120
-
Amide proton exchange in proteins by EX1 kinetics: Studies of the basic pancreatic trypsin inhibitor at variable pH and temperature
-
Roder H., Wagner G., Wüthrich K. Amide proton exchange in proteins by EX1 kinetics. studies of the basic pancreatic trypsin inhibitor at variable pH and temperature Biochemistry. 24:1985;7396-7407.
-
(1985)
Biochemistry
, vol.24
, pp. 7396-7407
-
-
Roder, H.1
Wagner, G.2
Wüthrich, K.3
-
12
-
-
0000857486
-
Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules
-
Otting G., Wüthrich K. Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Am. Chem. Soc. 111:1989;1871-1875.
-
(1989)
J. Am. Chem. Soc.
, vol.111
, pp. 1871-1875
-
-
Otting, G.1
Wüthrich, K.2
-
13
-
-
0026672305
-
NMR determination of residual structure in a urea-denatured protein, the 434 repressor
-
Neri D., Billeter M., Wider G., Wüthrich K. NMR determination of residual structure in a urea-denatured protein, the 434 repressor. Science. 257:1992;1559-1563.
-
(1992)
Science
, vol.257
, pp. 1559-1563
-
-
Neri, D.1
Billeter, M.2
Wider, G.3
Wüthrich, K.4
-
14
-
-
45249131217
-
1H NMR spectra of isotope-labeled proteins using X(ω1,ω2)-double-half-filter
-
1H NMR spectra of isotope-labeled proteins using X(ω1,ω2)-double-half-filter. J. Magn. Reson. 85:1989;586-594.
-
(1989)
J. Magn. Reson.
, vol.85
, pp. 586-594
-
-
Otting, G.1
Wüthrich, K.2
-
15
-
-
0025341339
-
15N spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
-
15N spectra of larger proteins. heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin Biochemistry. 29:1990;4659-4667.
-
(1990)
Biochemistry
, vol.29
, pp. 4659-4667
-
-
Ikura, M.1
Kay, L.E.2
Bax, A.3
-
16
-
-
0030722243
-
Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium
-
Tjandra N., Bax A. Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium. Science. 278:1997;1111-1114.
-
(1997)
Science
, vol.278
, pp. 1111-1114
-
-
Tjandra, N.1
Bax, A.2
-
17
-
-
0029050883
-
Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
-
Tolman J.R., Flanagan J.M., Kennedy M.A., Prestegard J.H. Nuclear magnetic dipole interactions in field-oriented proteins. information for structure determination in solution Proc. Natl. Acad. Sci. USA. 92:1995;9279-9283.
-
(1995)
Proc. Natl. Acad. Sci. USA.
, vol.92
, pp. 9279-9283
-
-
Tolman, J.R.1
Flanagan, J.M.2
Kennedy, M.A.3
Prestegard, J.H.4
-
18
-
-
0030612833
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA. 94:1997;12366-12371.
-
(1997)
Proc. Natl. Acad. Sci. USA.
, vol.94
, pp. 12366-12371
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wüthrich, K.4
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