-
1
-
-
0028274250
-
Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
-
Alexandrescu A. T., Abeygunawardana C., Shortle D. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. Biochemistry. 33:1994;1063-1072.
-
(1994)
Biochemistry
, vol.33
, pp. 1063-1072
-
-
Alexandrescu, A.T.1
Abeygunawardana, C.2
Shortle, D.3
-
2
-
-
0028806684
-
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: Implications for the initiation of protein folding
-
Arcus V. L., Vuilleumier S., Freund S. M. V., Bycroft M., Fersht A. R. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding. J. Mol. Biol. 254:1995;305-321.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 305-321
-
-
Arcus, V.L.1
Vuilleumier, S.2
Freund, S.M.V.3
Bycroft, M.4
Fersht, A.R.5
-
3
-
-
0010369733
-
NMR chemical shifts: A tool to characterize distortions of peptide and protein helices
-
Blanco F. L., Herranz L., González C., Jiménez- M. A., Rico M., Santoro J., Nieto J. L. NMR chemical shifts: a tool to characterize distortions of peptide and protein helices. J. Am. Chem. Soc. 114:1992;9676-9677.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 9676-9677
-
-
Blanco, F.L.1
Herranz, L.2
González, C.3
Jiménez-, M.A.4
Rico, M.5
Santoro, J.6
Nieto, J.L.7
-
4
-
-
0031160370
-
15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
-
15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure. J. Biomol. NMR. 9:1997;347-357.
-
(1997)
J. Biomol. NMR
, vol.9
, pp. 347-357
-
-
Blanco, F.L.1
Ortiz, A.R.2
Serrano, L.3
-
5
-
-
0000195671
-
Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
-
Bodenhausen G., Ruben D. J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69:1980;185-189.
-
(1980)
Chem. Phys. Lett
, vol.69
, pp. 185-189
-
-
Bodenhausen, G.1
Ruben, D.J.2
-
6
-
-
0031030716
-
Characterisation of the isolated Che Y C-terminal fragment (79-129)-Exploring the structure/stability/folding relationship of the α/β parallel protein Che Y
-
Bruix M., Munoz V., Campos-Olivas R., del Bosque J. R., Serrano L., Rico M. Characterisation of the isolated Che Y C-terminal fragment (79-129)-Exploring the structure/stability/folding relationship of the α/β parallel protein Che Y. Eur. J. Biochem. 243:1997;384-392.
-
(1997)
Eur. J. Biochem.
, vol.243
, pp. 384-392
-
-
Bruix, M.1
Munoz, V.2
Campos-Olivas, R.3
Del Bosque, J.R.4
Serrano, L.5
Rico, M.6
-
7
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio R., Grzesiek S., Vuister G. W., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;277-293.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, R.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
10
-
-
0031027137
-
Characterization of the backbone dynamics of folded and denatured states of an SH3 domain
-
Farrow N. A., Zhang O., Forman-Kay J. D., Kay L. E. Characterization of the backbone dynamics of folded and denatured states of an SH3 domain. Biochemistry. 36:1997;2390-2402.
-
(1997)
Biochemistry
, vol.36
, pp. 2390-2402
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
11
-
-
0028856785
-
Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
-
Fersht A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873.
-
(1995)
Proc. Natl Acad. Sci. USA
, vol.92
, pp. 10869-10873
-
-
Fersht, A.R.1
-
12
-
-
0000749460
-
Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements
-
Fiebig K. M., Schwalbe H., Buck M., Smith L. J., Dobson C. M. Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements. J. Phys. Chem. 100:1996;2661-2666.
-
(1996)
J. Phys. Chem.
, vol.100
, pp. 2661-2666
-
-
Fiebig, K.M.1
Schwalbe, H.2
Buck, M.3
Smith, L.J.4
Dobson, C.M.5
-
13
-
-
0000454610
-
HMQC-NOESY-HMQC, a three-dimensional NMR experiment which allows detection of nuclear Overhauser effects between protons with overlapping signals
-
Frenkiel T., Bauer C., Carr M. D., Birdsall B., Feeney J. HMQC-NOESY-HMQC, a three-dimensional NMR experiment which allows detection of nuclear Overhauser effects between protons with overlapping signals. J. Magn. Reson. 90:1990;420-425.
-
(1990)
J. Magn. Reson.
, vol.90
, pp. 420-425
-
-
Frenkiel, T.1
Bauer, C.2
Carr, M.D.3
Birdsall, B.4
Feeney, J.5
-
14
-
-
44949280676
-
Band-selective radiofrequency pulses
-
Geen H., Freeman R. Band-selective radiofrequency pulses. J. Magn. Reson. 93:1983;93-141.
-
(1983)
J. Magn. Reson.
, vol.93
, pp. 93-141
-
-
Geen, H.1
Freeman, R.2
-
15
-
-
0027787894
-
2O in protein NMR. Application to sensitivity enhancement and NOE measurements
-
2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115:1993;12593-12594.
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 12593-12594
-
-
Grzesiek, S.1
Bax, A.2
-
16
-
-
0031585992
-
Characterization of long range structure in the denatured state of Staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
-
Gillespie J., Shortle D. Characterization of long range structure in the denatured state of Staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 258:1997;170-184.
-
(1997)
J. Mol. Biol.
, vol.258
, pp. 170-184
-
-
Gillespie, J.1
Shortle, D.2
-
18
-
-
0027204024
-
Helix stop signals in proteins and peptides: The capping box
-
Harper E. T., Rose G. D. Helix stop signals in proteins and peptides: the capping box. Biochemistry. 32:1993;7605-7609.
-
(1993)
Biochemistry
, vol.32
, pp. 7605-7609
-
-
Harper, E.T.1
Rose, G.D.2
-
19
-
-
0001269119
-
Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy
-
Ikura M., Bax A., Clore G. M., Gronenborn A. M. Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 112:1990;9020-9022.
-
(1990)
J. Am. Chem. Soc.
, vol.112
, pp. 9020-9022
-
-
Ikura, M.1
Bax, A.2
Clore, G.M.3
Gronenborn, A.M.4
-
21
-
-
0026664396
-
Periodic properties of proton conformational shifts in isolated protein helices. An experimental study
-
Jiménez M. A., Blanco F. L., Rico M., Santoro L., Herranz J., Nieto J. L. Periodic properties of proton conformational shifts in isolated protein helices. An experimental study. Eur. J. Biochem. 207:1992;39-49.
-
(1992)
Eur. J. Biochem.
, vol.207
, pp. 39-49
-
-
Jiménez, M.A.1
Blanco, F.L.2
Rico, M.3
Santoro, L.4
Herranz, J.5
Nieto, J.L.6
-
22
-
-
34249765651
-
NMRView: A computer program for the visualization and analysis of NMR data
-
Johnson B. A., Blevins R. A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 603-614
-
-
Johnson, B.A.1
Blevins, R.A.2
-
23
-
-
44949291986
-
Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
-
Kay L. E., Ikura M., Tschudin R., Bax A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89:1990;496-514.
-
(1990)
J. Magn. Reson.
, vol.89
, pp. 496-514
-
-
Kay, L.E.1
Ikura, M.2
Tschudin, R.3
Bax, A.4
-
24
-
-
0006925492
-
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
-
Kay L. E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 10663-10665
-
-
Kay, L.E.1
Keifer, P.2
Saarinen, T.3
-
26
-
-
0026244229
-
Molscript: A program to produce both detailed and schematic plots of protein structures
-
Kraulis P. J. Molscript: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
-
(1991)
J. Appl. Crystallog.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
27
-
-
0028297302
-
Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride
-
Logan T. M., Theriault Y., Fesik S. W. Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol. 236:1994;637-648.
-
(1994)
J. Mol. Biol.
, vol.236
, pp. 637-648
-
-
Logan, T.M.1
Theriault, Y.2
Fesik, S.W.3
-
28
-
-
0027391780
-
Capping interactions in isolated α helices: Position-dependent substitution effects and structure of a serine-capped peptide helix
-
Lyu P. C., Wemmer D. E., Zhou H. X., Pinker R. J., Kallenbach N. R. Capping interactions in isolated α helices: position-dependent substitution effects and structure of a serine-capped peptide helix. Biochemistry. 32:1993;421-425.
-
(1993)
Biochemistry
, vol.32
, pp. 421-425
-
-
Lyu, P.C.1
Wemmer, D.E.2
Zhou, H.X.3
Pinker, R.J.4
Kallenbach, N.R.5
-
29
-
-
0029207339
-
1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
-
1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR. 5:1995;14-24.
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 14-24
-
-
Merutka, G.1
Dyson, H.J.2
Wright, P.E.3
-
30
-
-
0001689741
-
Gradient-enhanced triple-resonance three dimensional NMR experiments with improved sensitivity
-
Muhandiram D. R., Kay L. E. Gradient-enhanced triple-resonance three dimensional NMR experiments with improved sensitivity. J. Magn. Reson ser. B. 103:1994;203-216.
-
(1994)
J. Magn. Reson Ser. B
, vol.103
, pp. 203-216
-
-
Muhandiram, D.R.1
Kay, L.E.2
-
31
-
-
0028447768
-
Elucidating the folding problem of helical peptides using empirical parameters
-
Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 1:1994;399-409.
-
(1994)
Nature Struct. Biol.
, vol.1
, pp. 399-409
-
-
Muñoz, V.1
Serrano, L.2
-
32
-
-
0028873081
-
Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
-
Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245:1995;275-296.
-
(1995)
J. Mol. Biol.
, vol.245
, pp. 275-296
-
-
Muñoz, V.1
Serrano, L.2
-
33
-
-
0026437577
-
Crystal structure of a Src-homology 3 (SH3) domain
-
Musacchio A., Noble M., Pauptit R., Wider R., Saraste M. Crystal structure of a Src-homology 3 (SH3) domain. Nature. 359:1992;851-855.
-
(1992)
Nature
, vol.359
, pp. 851-855
-
-
Musacchio, A.1
Noble, M.2
Pauptit, R.3
Wider, R.4
Saraste, M.5
-
34
-
-
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
-
35
-
-
0031574916
-
Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain
-
Prieto L., Wilmans M., Jimenez M. A., Rico M., Serrano L. Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain. J. Mol. Biol. 268:1997;760-778.
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 760-778
-
-
Prieto, L.1
Wilmans, M.2
Jimenez, M.A.3
Rico, M.4
Serrano, L.5
-
36
-
-
0001935783
-
Quantitative evaluation of interproton distances in peptides by two-dimensional Overhauser effect spectroscopy
-
Saulitis J., Liepins E. Quantitative evaluation of interproton distances in peptides by two-dimensional Overhauser effect spectroscopy. J. Magn. Reson. 74:1990;80-91.
-
(1990)
J. Magn. Reson.
, vol.74
, pp. 80-91
-
-
Saulitis, J.1
Liepins, E.2
-
37
-
-
0028389502
-
A general enhancement scheme in heteronuclear multidimensionnal NMR employing pulsed field gradients
-
Schleucher L., Schwendiger M., Sattler M., Schmidt P., Schedletzky O., Glaser S. L., Sørensen O. W., Griesinger C. A general enhancement scheme in heteronuclear multidimensionnal NMR employing pulsed field gradients. J. Biomol. NMR. 5:1994;301-306.
-
(1994)
J. Biomol. NMR
, vol.5
, pp. 301-306
-
-
Schleucher, L.1
Schwendiger, M.2
Sattler, M.3
Schmidt, P.4
Schedletzky, O.5
Glaser, S.L.6
Sørensen, O.W.7
Griesinger, C.8
-
38
-
-
0028790273
-
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation
-
Serrano L. Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation. J. Mol. Biol. 254:1995;322-333.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 322-333
-
-
Serrano, L.1
-
39
-
-
0027394283
-
Denatured states of proteins and their roles in folding and stability
-
Shortle D. Denatured states of proteins and their roles in folding and stability. Curr. Opin. Struct. Biol. 3:1993;66-74.
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 66-74
-
-
Shortle, D.1
-
41
-
-
0030663205
-
Loop length, intramolecular diffusion and protein folding
-
Viguera A. R., Serrano L. Loop length, intramolecular diffusion and protein folding. Nature Struct. Biol. 4:1997;939-946.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 939-946
-
-
Viguera, A.R.1
Serrano, L.2
-
42
-
-
0028331876
-
Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
-
Viguera A. R., Martínez J. C., Filimonov V. V., Mateo P. L., Serrano L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry. 33:1994;2142-2150.
-
(1994)
Biochemistry
, vol.33
, pp. 2142-2150
-
-
Viguera, A.R.1
Martínez, J.C.2
Filimonov, V.V.3
Mateo, P.L.4
Serrano, L.5
-
43
-
-
0343059020
-
Conformational analysis of peptides corresponding to β-hairpins and a β-sheet that represent the entire sequence of the α-spectrin SH3 domain
-
Viguera A. R., Jiménez- M. A., Rico M., Serrano L. Conformational analysis of peptides corresponding to β-hairpins and a β-sheet that represent the entire sequence of the α-spectrin SH3 domain. J. Mol. Biol. 255:1996a;507-521.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 507-521
-
-
Viguera, A.R.1
Jiménez-, M.A.2
Rico, M.3
Serrano, L.4
-
44
-
-
0029760326
-
Different folding transition states may result in the same native structure
-
Viguera A. R., Serrano L., Wilmanns M. Different folding transition states may result in the same native structure. Nature Struct. Biol. 3:1996b;874-880.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 874-880
-
-
Viguera, A.R.1
Serrano, L.2
Wilmanns, M.3
-
46
-
-
0025328818
-
Secondary-structure dependent chemical shifts in proteins
-
Williamson M. P. Secondary-structure dependent chemical shifts in proteins. Biopolymers. 9:1990;1423-1431.
-
(1990)
Biopolymers
, vol.9
, pp. 1423-1431
-
-
Williamson, M.P.1
-
47
-
-
0026410969
-
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
-
Wishart D. S., Sykes B. D., Richards F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:1991;311-333.
-
(1991)
J. Mol. Biol.
, vol.222
, pp. 311-333
-
-
Wishart, D.S.1
Sykes, B.D.2
Richards, F.M.3
-
49
-
-
43949167657
-
HNCACB, a high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α- and β-carbon resonances in proteins
-
Wittekind M., Müeller L. HNCACB, a high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α- and β-carbon resonances in proteins. J. Magn. Reson. ser. B. 101:1993;201-205.
-
(1993)
J. Magn. Reson. Ser. B
, vol.101
, pp. 201-205
-
-
Wittekind, M.1
Müeller, L.2
-
50
-
-
0030596513
-
13C NMR assignment and characterisation of residual structure
-
13C NMR assignment and characterisation of residual structure. J. Biomol. NMR. 259:1996;805-818.
-
(1996)
J. Biomol. NMR
, vol.259
, pp. 805-818
-
-
Wong, K.B.1
Freund, S.M.2
Fersht, A.R.3
-
52
-
-
0027955640
-
NMR assignments as a basis for structural characterization of denatured states of globular proteins
-
Wüthrich K. NMR assignments as a basis for structural characterization of denatured states of globular proteins. Curr. Opin. Struct. Biol. 4:1994;93-99.
-
(1994)
Curr. Opin. Struct. Biol.
, vol.4
, pp. 93-99
-
-
Wüthrich, K.1
-
53
-
-
0029036496
-
Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer
-
Zhang O., Forman-Kay J. D. Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer. Biochemistry. 34:1995;6784-6794.
-
(1995)
Biochemistry
, vol.34
, pp. 6784-6794
-
-
Zhang, O.1
Forman-Kay, J.D.2
-
54
-
-
0030900199
-
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions
-
Zhang O., Forman-Kay J. D. NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions. Biochemistry. 36:1997;3959-3970.
-
(1997)
Biochemistry
, vol.36
, pp. 3959-3970
-
-
Zhang, O.1
Forman-Kay, J.D.2
-
55
-
-
0028541866
-
15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradients NMR techniques
-
15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradients NMR techniques. J. Biomol. NMR. 4:1994;845-858.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 845-858
-
-
Zhang, O.1
Kay, L.E.2
Olivier, J.P.3
Forman-Kay, J.D.4
-
56
-
-
0031064317
-
Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
-
Zhang O., Forman-Kay J. D., Shortle D., Kay L. E. Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins. J. Biomol. NMR. 9:1997a;181-200.
-
(1997)
J. Biomol. NMR
, vol.9
, pp. 181-200
-
-
Zhang, O.1
Forman-Kay, J.D.2
Shortle, D.3
Kay, L.E.4
-
57
-
-
0031565731
-
Comprehensive NOE characterization of a partially folded large fragment of staphyococcal nuclease, Δ131Δ, using NMR methods with improved resolution
-
Zhang O., Kay L. E., Shortle D., Forman-Kay J. D. Comprehensive NOE characterization of a partially folded large fragment of staphyococcal nuclease, Δ131Δ, using NMR methods with improved resolution. J. Mol. Biol. 272:1997b;9-20.
-
(1997)
J. Mol. Biol.
, vol.272
, pp. 9-20
-
-
Zhang, O.1
Kay, L.E.2
Shortle, D.3
Forman-Kay, J.D.4
|