-
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. (1995). 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, 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
-
4
-
-
12044252858
-
Methodological advances in protein NMR
-
Bax, A. & Grzesiek, S. (1993). Methodological advances in protein NMR. Ace. Chem. Res. 26, 131-138.
-
(1993)
Ace. Chem. Res.
, vol.26
, pp. 131-138
-
-
Bax, A.1
Grzesiek, S.2
-
5
-
-
0030623419
-
Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the alpha-helix fragment
-
Blanco, F. J., Ortiz, A. R. & Serrano, L. (1997). Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the alpha-helix fragment. Folding Des. 2, 123-133.
-
(1997)
Folding Des.
, vol.2
, pp. 123-133
-
-
Blanco, F.J.1
Ortiz, A.R.2
Serrano, L.3
-
6
-
-
0000195671
-
Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
-
Bodenhausen, G. & Ruben, D. L. (1980). Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters, 69, 185-188.
-
(1980)
Chem. Phys. Letters
, vol.69
, pp. 185-188
-
-
Bodenhausen, G.1
Ruben, D.L.2
-
8
-
-
0027405357
-
Cooperativity in protein-folding kinetics
-
Dill, K. A., Fiebig, K. M. & Chan, H. S. (1993). Cooperativity in protein-folding kinetics. Proc. Natl Acad. Sci. USA, 90, 1942-1946.
-
(1993)
Proc. Natl Acad. Sci. USA
, vol.90
, pp. 1942-1946
-
-
Dill, K.A.1
Fiebig, K.M.2
Chan, H.S.3
-
9
-
-
0001931668
-
Unfolded proteins, compact states and molten globules
-
Dobson, C. M. (1992). Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2, 6-12.
-
(1992)
Curr. Opin. Struct. Biol.
, vol.2
, pp. 6-12
-
-
Dobson, C.M.1
-
10
-
-
0003170076
-
An alternative method for distance evaluation from NOESY spectra
-
Esposito, G. & Pastore, A. (1988). An alternative method for distance evaluation from NOESY spectra. J. Magn. Reson. 76, 331-336.
-
(1988)
J. Magn. Reson.
, vol.76
, pp. 331-336
-
-
Esposito, G.1
Pastore, A.2
-
11
-
-
0028951040
-
Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffers
-
Farrow, N. A., Zhang, O., Forman-Kay, J. D. & Kay, L. E. (1995). Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffers. Biochemistry, 34, 868-878.
-
(1995)
Biochemistry
, vol.34
, pp. 868-878
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
12
-
-
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. (1997). Characterization of the backbone dynamics of folded and denatured states of an SH3 domain. Biochemistry, 36, 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
-
13
-
-
0026019655
-
Rate of β-structure formation in polypeptides
-
Finkelstein, A. V. (1991). Rate of β-structure formation in polypeptides. Proteins: Struct. Funct. Genet. 9, 23-27.
-
(1991)
Proteins: Struct. Funct. Genet.
, vol.9
, pp. 23-27
-
-
Finkelstein, A.V.1
-
14
-
-
0030573054
-
Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans
-
Fong, S., Hamill, S. J., Proctor, M., Freund, S. M. V., Benian, G. M., Chothia, C., Bycroft, M. & Clarke, J. (1996). Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J. Mol. Biol. 264, 624-639.
-
(1996)
J. Mol. Biol.
, vol.264
, pp. 624-639
-
-
Fong, S.1
Hamill, S.J.2
Proctor, M.3
Freund, S.M.V.4
Benian, G.M.5
Chothia, C.6
Bycroft, M.7
Clarke, J.8
-
15
-
-
0028787226
-
Structural and dynamic characterisation of the urea denatured state of the immunoglobulin binding domain of streptococcal protein by mutidimensional heteronuclear NMR spectroscopy
-
Frank, M. K., Clore, G. M. & Gronenborn, A. M. (1995). Structural and dynamic characterisation of the urea denatured state of the immunoglobulin binding domain of streptococcal protein by mutidimensional heteronuclear NMR spectroscopy. Protein Sci. 4, 2605-2615.
-
(1995)
Protein Sci.
, vol.4
, pp. 2605-2615
-
-
Frank, M.K.1
Clore, G.M.2
Gronenborn, A.M.3
-
16
-
-
0029784407
-
Initiation sites of protein folding by NMR analysis
-
Freund, S. M. V., Wong, K. B. & Fersht, A. R. (1996). Initiation sites of protein folding by NMR analysis. Proc. Natl Acad. Sci. USA, 93, 10600-10603.
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 10600-10603
-
-
Freund, S.M.V.1
Wong, K.B.2
Fersht, A.R.3
-
17
-
-
44049117010
-
Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
-
Grzesiek, S. & Bax, A. (1992). Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96, 432-440.
-
(1992)
J. Magn. Reson.
, vol.96
, pp. 432-440
-
-
Grzesiek, S.1
Bax, A.2
-
18
-
-
0027569483
-
Amino-acid type determination in the sequential assignment procedure of uniformly C-13/N15-enriched proteins
-
Grzesiek, S. & Bax, A. (1993). Amino-acid type determination in the sequential assignment procedure of uniformly C-13/N15-enriched proteins. J. Biomol. NMR, 3, 185-204.
-
(1993)
J. Biomol. NMR
, vol.3
, pp. 185-204
-
-
Grzesiek, S.1
Bax, A.2
-
19
-
-
0001269119
-
Detection of nuclear overhauser effects between degenerate amide proton resonances by heteronuclear 3-dimensional nuclear-magnetic-resonance spectroscopy
-
Ikura, M., Bax, A., Clore, G. M. & Gronenborn, A. M. (1990). Detection of nuclear overhauser effects between degenerate amide proton resonances by heteronuclear 3-dimensional nuclear-magnetic-resonance spectroscopy. J. Am. Chem. Soc. 112, 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
-
20
-
-
0028938022
-
Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei
-
Ishima, R. & Nagayama, K. (1995). Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei. Biochemistry, 34, 3162-3171.
-
(1995)
Biochemistry
, vol.34
, pp. 3162-3171
-
-
Ishima, R.1
Nagayama, K.2
-
21
-
-
0030624544
-
NMR methods for the study of protein structure and dynamics
-
Kay, L. E. (1997). NMR methods for the study of protein structure and dynamics. Biochem. Cell Biol. 75, 1-15.
-
(1997)
Biochem. Cell Biol.
, vol.75
, pp. 1-15
-
-
Kay, L.E.1
-
22
-
-
0024449503
-
15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
-
15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry, 28, 8972-8979.
-
(1989)
Biochemistry
, vol.28
, pp. 8972-8979
-
-
Kay, L.E.1
Torchia, D.A.2
Bax, A.3
-
23
-
-
0006925492
-
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
-
Kay, L. E., Keifer, P. & Saarinen, T. (1992). Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 10663-10665
-
-
Kay, L.E.1
Keifer, P.2
Saarinen, T.3
-
24
-
-
0028297302
-
Structural characterisation of the FK506 binding protein unfolded in urea and guanidine hydrochloride
-
Logan, T. M., Thériault, Y. & Fesik, S. W. (1994). Structural characterisation of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol. 236, 637-648.
-
(1994)
J. Mol. Biol.
, vol.236
, pp. 637-648
-
-
Logan, T.M.1
Thériault, Y.2
Fesik, S.W.3
-
25
-
-
84915716471
-
Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
-
Macura, S. & Ernst, R. R. (1980). Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41, 95-117.
-
(1980)
Mol. Phys.
, vol.41
, pp. 95-117
-
-
Macura, S.1
Ernst, R.R.2
-
26
-
-
0024362326
-
15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy. Application to interleukin 1β
-
15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy. Application to interleukin 1β. Biochemistry, 28, 6150-6156.
-
(1989)
Biochemistry
, vol.28
, pp. 6150-6156
-
-
Marion, D.1
Driscoll, P.C.2
Kay, L.E.3
Wingfield, P.T.4
Bax, A.5
Gronenborn, A.M.6
Clore, G.M.7
-
27
-
-
0026524680
-
2H exchange nuclear magnetic resonance studies of the folding pathway of barnase- Complementary to and agreement with protein engineering studies
-
2H exchange nuclear magnetic resonance studies of the folding pathway of barnase- complementary to and agreement with protein engineering studies. J. Mol. Biol. 224, 837-845.
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 837-845
-
-
Matouschek, A.1
Serrano, L.2
Meiering, E.M.3
Bycroft, M.4
Fersht, A.R.5
-
28
-
-
0029207339
-
Random coil H-1 chemical-shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
-
Merutka, G., Dyson, H. J. & Wright, P. E. (1995). Random coil H-1 chemical-shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR, 5, 14-24.
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 14-24
-
-
Merutka, G.1
Dyson, H.J.2
Wright, P.E.3
-
29
-
-
0025906759
-
An analysis of protein folding pathways
-
Moult, J. & Unger, R. (1991). An analysis of protein folding pathways. Biochemistry, 30, 3816-3824.
-
(1991)
Biochemistry
, vol.30
, pp. 3816-3824
-
-
Moult, J.1
Unger, R.2
-
30
-
-
0026672305
-
NMR determination of residual structure in a urea-denatured protein, the 434-repressor
-
Neri, D., Billeter, M., Wider, G. & Wüthrich, K. (1992). NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science, 257, 1559-1563.
-
(1992)
Science
, vol.257
, pp. 1559-1563
-
-
Neri, D.1
Billeter, M.2
Wider, G.3
Wüthrich, K.4
-
31
-
-
0031019924
-
The folding pathway of a protein at high resolution from micro-seconds to seconds
-
Nölting, B., Golbik, R., Neira, J. L., Soler-Gonzalez, A. S., Schreiber, G. & Fersht, A. R. (1997). The folding pathway of a protein at high resolution from micro-seconds to seconds. Proc. Natl Acad. Sci. USA, 94, 826-830.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 826-830
-
-
Nölting, B.1
Golbik, R.2
Neira, J.L.3
Soler-Gonzalez, A.S.4
Schreiber, G.5
Fersht, A.R.6
-
32
-
-
0000660936
-
Mapping of spectral density-functions using heteronuclear NMR relaxation measurements
-
Peng, J. W. & Wagner, G. (1992a). Mapping of spectral density-functions using heteronuclear NMR relaxation measurements. J. Magn. Reson. 98, 308-332.
-
(1992)
J. Magn. Reson.
, vol.98
, pp. 308-332
-
-
Peng, J.W.1
Wagner, G.2
-
33
-
-
0026784152
-
Mapping of the spectral densities of N-H bond motions in Eglin-c using heteronuclear relaxation experiments
-
Peng, J. W. & Wagner, G. (1992b). Mapping of the spectral densities of N-H bond motions in Eglin-c using heteronuclear relaxation experiments. Biochemistry, 31, 8571-8586.
-
(1992)
Biochemistry
, vol.31
, pp. 8571-8586
-
-
Peng, J.W.1
Wagner, G.2
-
34
-
-
0028674384
-
Investigation of protein motions via relaxation measurements
-
Peng, J. W. & Wagner, G. (1994). Investigation of protein motions via relaxation measurements. Methods Enzymol. 239, 563-596.
-
(1994)
Methods Enzymol.
, vol.239
, pp. 563-596
-
-
Peng, J.W.1
Wagner, G.2
-
35
-
-
0029623152
-
Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
-
Peng, J. W. & Wagner, G. (1995). Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields. Biochemistry, 34, 16733-16752.
-
(1995)
Biochemistry
, vol.34
, pp. 16733-16752
-
-
Peng, J.W.1
Wagner, G.2
-
36
-
-
0026951903
-
Gradient-tailored excitation for single-quantum NMR spectroscopy of acqueous solutions
-
Piotto, M., Saudek, V. & Sklenar, V. (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of acqueous solutions. J. Biomol. NMR, 2, 661-665.
-
(1992)
J. Biomol. NMR
, vol.2
, pp. 661-665
-
-
Piotto, M.1
Saudek, V.2
Sklenar, V.3
-
37
-
-
0031574916
-
Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all beta-sheet alpha-spectrin SH3 domain
-
Prieto, J., Wilmans, M., Jiménez, M. A., Rico, M. & Serrano, L. (1997). Non-native local interactions in protein folding and stability: introducing a helical tendency in the all beta-sheet alpha-spectrin SH3 domain. J. Mol. Biol. 268, 760-778.
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 760-778
-
-
Prieto, J.1
Wilmans, M.2
Jiménez, M.A.3
Rico, M.4
Serrano, L.5
-
38
-
-
0026731991
-
Hydrogen exchange in native and denatured states of hen egg-white lysozyme
-
D., T. K.
-
Radford, S. E., Buck, M., D., T. K., Dobson, C. M. & Evans, P. A. (1992). Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins: Struct. Funct. Genet. 14, 237-248.
-
(1992)
Proteins: Struct. Funct. Genet.
, vol.14
, pp. 237-248
-
-
Radford, S.E.1
Buck, M.2
Dobson, C.M.3
Evans, P.A.4
-
39
-
-
0024331090
-
Structural characterisation of protein folding intermediates by proton magnetic resonance and hydrogen exchange
-
Roder, H. (1989). Structural characterisation of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol. 176, 446-473.
-
(1989)
Methods Enzymol.
, vol.176
, pp. 446-473
-
-
Roder, H.1
-
40
-
-
0001935783
-
Quantitative evaluation of interproton distances in peptides by two-dimensional Overhauser effect spectroscopy
-
Saulitis, J. & Liepins, E. (1990). Quantitative evaluation of interproton distances in peptides by two-dimensional Overhauser effect spectroscopy. J. Magn. Reson. 87, 80-91.
-
(1990)
J. Magn. Reson.
, vol.87
, pp. 80-91
-
-
Saulitis, J.1
Liepins, E.2
-
41
-
-
0041089466
-
Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: Evidence for hairpins as initiation sites for β-sheet formation
-
Schönbrunner, N., Pappenberger, G., Scharf, M., Engels, J. & Kiefhaber, T. (1997). Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for β-sheet formation. Biochemistry, 36, 9057-9065.
-
(1997)
Biochemistry
, vol.36
, pp. 9057-9065
-
-
Schönbrunner, N.1
Pappenberger, G.2
Scharf, M.3
Engels, J.4
Kiefhaber, T.5
-
42
-
-
0026563495
-
The folding of an enzyme. 6. The folding pathway of barnase-comparison with theoretical models
-
Serrano, L., Matouschek, A. & Fersht, A. R. (1992). The folding of an enzyme. 6. The folding pathway of barnase-comparison with theoretical models. J. Mol. Biol. 224, 847-859.
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 847-859
-
-
Serrano, L.1
Matouschek, A.2
Fersht, A.R.3
-
43
-
-
0027394283
-
Denatured states of proteins and their roles in folding and stability
-
Shortle, D. (1993). Denatured states of proteins and their roles in folding and stability. Curr. Opin. Struct. Biol. 3, 66-74.
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 66-74
-
-
Shortle, D.1
-
44
-
-
0030032461
-
The denatured state (the other half of the folding equation) and its role in protein stability
-
Shortle, D. (1996a). The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10, 27-34.
-
(1996)
FASEB J.
, vol.10
, pp. 27-34
-
-
Shortle, D.1
-
45
-
-
0029961647
-
Structural-analysis of nonnative states of proteins by NMR methods
-
Shortle, D. (1996b). Structural-analysis of nonnative states of proteins by NMR methods. Curr. Opin. Struct. Biol. 6, 24-30.
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 24-30
-
-
Shortle, D.1
-
46
-
-
0029978353
-
Analysis of main-chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
-
Smith, L. J., Bolin, K. A., Schwalbe, H., MacArthur, M. W., Thornton, J. M. & Dobson, C. M. (1996). Analysis of main-chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255, 494-506.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 494-506
-
-
Smith, L.J.1
Bolin, K.A.2
Schwalbe, H.3
MacArthur, M.W.4
Thornton, J.M.5
Dobson, C.M.6
-
47
-
-
0002584387
-
A convenient and accurate method for the measurement of the values of spin-spin coupling-constants
-
Stonehouse, J. & Keeler, J. (1995). A convenient and accurate method for the measurement of the values of spin-spin coupling-constants. J. Magn. Reson. 112, 43-47.
-
(1995)
J. Magn. Reson.
, vol.112
, pp. 43-47
-
-
Stonehouse, J.1
Keeler, J.2
-
48
-
-
0027190613
-
Kinetics of folding of the all-β sheet protein interleukin-1β
-
Varley, P., Gronenborn, A. M., Christensen, H., Wingfield, P. T., Pain, R. H. & Clore, G. M. (1993). Kinetics of folding of the all-β sheet protein interleukin-1β. Science, 260, 1110-1113.
-
(1993)
Science
, vol.260
, pp. 1110-1113
-
-
Varley, P.1
Gronenborn, A.M.2
Christensen, H.3
Wingfield, P.T.4
Pain, R.H.5
Clore, G.M.6
-
49
-
-
0028856228
-
The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
-
Wang, Y. & Shortle, D. (1995). The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy. Biochemistry, 34, 15895-15905.
-
(1995)
Biochemistry
, vol.34
, pp. 15895-15905
-
-
Wang, Y.1
Shortle, D.2
-
52
-
-
0027955640
-
NMR assignment as a basis for structural characterisation of denatured states of globular-proteins
-
Wüthrich, K. (1994). NMR assignment as a basis for structural characterisation of denatured states of globular-proteins. Curr. Opin. Struct. Biol. 4, 93-99.
-
(1994)
Curr. Opin. Struct. Biol.
, vol.4
, pp. 93-99
-
-
Wüthrich, K.1
-
53
-
-
0031064317
-
Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterisation of unfolded, partially folded and folded proteins
-
Zhang, O. W., Forman-Kay, J. D., Shortle, D. & Kay, L. E. (1997). Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterisation of unfolded, partially folded and folded proteins. J. Biomol. NMR, 9, 181-200.
-
(1997)
J. Biomol. NMR
, vol.9
, pp. 181-200
-
-
Zhang, O.W.1
Forman-Kay, J.D.2
Shortle, D.3
Kay, L.E.4
|