-
1
-
-
0027313673
-
Pathways of protein folding
-
Matthews, C.R. Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683 (1993).
-
(1993)
Annu. Rev. Biochem.
, vol.62
, pp. 653-683
-
-
Matthews, C.R.1
-
2
-
-
0029249945
-
The nature of protein folding pathways: The classical versus the new view
-
Baldwin, R.L. The nature of protein folding pathways: the classical versus the new view. J. Biomol. NMR 5, 103-109 (1995).
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 103-109
-
-
Baldwin, R.L.1
-
3
-
-
0028958601
-
Characterizing transition states in protein folding: An essential step in the puzzle
-
Fersht, A.R. Characterizing transition states in protein folding: An essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79-84 (1995).
-
(1995)
Curr. Opin. Struct. Biol.
, vol.5
, pp. 79-84
-
-
Fersht, A.R.1
-
4
-
-
0030330918
-
Insights into protein folding from NMR
-
Dyson, H.J. & Wright, P.E. Insights into protein folding from NMR. Ann. Rev. Phys. Chem. 47, 369-395 (1996).
-
(1996)
Ann. Rev. Phys. Chem.
, vol.47
, pp. 369-395
-
-
Dyson, H.J.1
Wright, P.E.2
-
5
-
-
0028947257
-
Funnels, pathways, and the energy landscape of protein folding: A synthesis
-
Bryngelson, J.D., Onuchic. J.N., Socci, N.D. & Wolynes, P.G. Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21, 167-195 (1995).
-
(1995)
Proteins
, vol.21
, pp. 167-195
-
-
Bryngelson, J.D.1
Onuchic, J.N.2
Socci, N.D.3
Wolynes, P.G.4
-
6
-
-
0028924552
-
Navigating the folding routes
-
Wolynes, P.G., Onuchic, J.N. & Thirumalai, D. Navigating the folding routes. Science 267, 1619-1620 (1995).
-
(1995)
Science
, vol.267
, pp. 1619-1620
-
-
Wolynes, P.G.1
Onuchic, J.N.2
Thirumalai, D.3
-
7
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings, P.A. & Wright, P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896 (1993).
-
(1993)
Science
, vol.262
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
8
-
-
0029014386
-
Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
-
Loh, S.N., Kay, M.S. & Baldwin, R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway-Proc. Natl. Acad. Sci. USA 92, 5446-5450 (1995).
-
(1995)
Proc. Natl. Acad. Sci. USA
, vol.92
, pp. 5446-5450
-
-
Loh, S.N.1
Kay, M.S.2
Baldwin, R.L.3
-
9
-
-
0023759595
-
Thermodynamic study of the apomyoglobin structure
-
Griko, Y.V., Privalov, P.L, Venyaminov, S.Y. & Kutyshenko, V.P. Thermodynamic study of the apomyoglobin structure. J. Mol. Biol. 202, 127-138 (1988).
-
(1988)
J. Mol. Biol.
, vol.202
, pp. 127-138
-
-
Griko, Y.V.1
Privalov, P.L.2
Venyaminov, S.Y.3
Kutyshenko, V.P.4
-
10
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson, F.M., Wright, P.E. & Baldwin, R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science 249, 1544-1548 (1990).
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
11
-
-
0028884580
-
The radius of gyration of an apomyoglobin folding intermediate
-
Eliezer, D. et al.The radius of gyration of an apomyoglobin folding intermediate. Science 270, 487-488 (1995).
-
(1995)
Science
, vol.270
, pp. 487-488
-
-
Eliezer, D.1
-
12
-
-
0030575785
-
Is apomyoglobin a molten globule? Structural characterization by NMR
-
Eliezer, D. & Wright, P.E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263, 531-538 (1996).
-
(1996)
J. Mol. Biol.
, vol.263
, pp. 531-538
-
-
Eliezer, D.1
Wright, P.E.2
-
13
-
-
0028329347
-
Thermodynamic puzzle of apomyoglobin unfolding
-
Griko, Y.V. & Privalov, P.L Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol. 235, 1318-1325 (1994).
-
(1994)
J. Mol. Biol.
, vol.235
, pp. 1318-1325
-
-
Griko, Y.V.1
Privalov, P.L.2
-
14
-
-
0030726758
-
Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for characterization by NMR
-
Eliezer, D., Jennings, P.A., Dyson, H.J. & Wright, P.E. Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for characterization by NMR. FEBS Lett. 417, 92-96 (1997).
-
(1997)
FEBS Lett.
, vol.417
, pp. 92-96
-
-
Eliezer, D.1
Jennings, P.A.2
Dyson, H.J.3
Wright, P.E.4
-
15
-
-
0024293204
-
Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
-
Wright, P.E., Dyson, H.J. & Lerner, R.A. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry 27, 7167-7175 (1988).
-
(1988)
Biochemistry
, vol.27
, pp. 7167-7175
-
-
Wright, P.E.1
Dyson, H.J.2
Lerner, R.A.3
-
16
-
-
0028243107
-
Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
-
Nishii, I., Kataoka, M., Tokunaga, F. & Goto, Y. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 33, 4903-4909 (1994).
-
(1994)
Biochemistry
, vol.33
, pp. 4903-4909
-
-
Nishii, I.1
Kataoka, M.2
Tokunaga, F.3
Goto, Y.4
-
17
-
-
0025616115
-
Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study
-
Cocco, M.J. & Lecomte, J.TJ. Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study. Biochemistry 29, 11067-11072 (1990).
-
(1990)
Biochemistry
, vol.29
, pp. 11067-11072
-
-
Cocco, M.J.1
Lecomte, J.T.J.2
-
18
-
-
0030056766
-
The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
-
Lecomte, J.T.J., Kao, Y.H. & Cocco, M.J. The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins 25, 267-285 (1996).
-
(1996)
Proteins
, vol.25
, pp. 267-285
-
-
Lecomte, J.T.J.1
Kao, Y.H.2
Cocco, M.J.3
-
19
-
-
0029400889
-
Overexpression of myoglobin and assignment of the amide, Cα and Cβ resonances
-
Jennings, P.A., Stone, M.J. & Wright, P.E. Overexpression of myoglobin and assignment of the amide, Cα and Cβ resonances. J. Biomol. NMR 6, 271-276 (1995).
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 271-276
-
-
Jennings, P.A.1
Stone, M.J.2
Wright, P.E.3
-
20
-
-
0000084729
-
Sequence-corrected 15N "random coil" chemical shifts
-
Braun, D., Wider, G. & Wüthrich, K. Sequence-corrected 15N "random coil" chemical shifts. J. Am. Chem. Soc. 116, 3466-8469 (1994).
-
(1994)
J. Am. Chem. Soc.
, vol.116
, pp. 3466-8469
-
-
Braun, D.1
Wider, G.2
Wüthrich, K.3
-
21
-
-
0031451750
-
Chemical shift dispersion and secondary structure prediction in unfolded and partly-folded proteins
-
Yao, J., Dyson, H.J. & Wright, P.E. Chemical shift dispersion and secondary structure prediction in unfolded and partly-folded proteins. FEBS Lett 419, 285-289 (1997).
-
(1997)
FEBS Lett
, vol.419
, pp. 285-289
-
-
Yao, J.1
Dyson, H.J.2
Wright, P.E.3
-
22
-
-
0031565731
-
Comprehensive NOE characterization of a partly folded large fragment of staphylococcal nuclease D131D, using NMR methods with improved resolution
-
Zhang, O., Kay, I.E., Shortle, D. & Forman-Kay, J.D. Comprehensive NOE characterization of a partly folded large fragment of staphylococcal nuclease D131D, using NMR methods with improved resolution. J. Mol. Biol. 272, 9-20 (1997).
-
(1997)
J. Mol. Biol.
, vol.272
, pp. 9-20
-
-
Zhang, O.1
Kay, I.E.2
Shortle, D.3
Forman-Kay, J.D.4
-
23
-
-
0028674451
-
Multidimensional heteronudear nuclear magnetic resonance of proteins
-
Clore, G.M. & Gronenborn, A.M. Multidimensional heteronudear nuclear magnetic resonance of proteins. Meth. Enz. 239, 349-363 (1994).
-
(1994)
Meth. Enz.
, vol.239
, pp. 349-363
-
-
Clore, G.M.1
Gronenborn, A.M.2
-
24
-
-
0024533979
-
Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig a-lactalbumin
-
Baum, J., Dobson, C.M., Evans, P.A. & Hanley, C. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig a-lactalbumin. Biochemistry 28, 7-13 (1989).
-
(1989)
Biochemistry
, vol.28
, pp. 7-13
-
-
Baum, J.1
Dobson, C.M.2
Evans, P.A.3
Hanley, C.4
-
25
-
-
0027536094
-
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study
-
Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J. & Dobson, C.M. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study. Biochemistry 32, 1707-1718 (1993).
-
(1993)
Biochemistry
, vol.32
, pp. 1707-1718
-
-
Alexandrescu, A.T.1
Evans, P.A.2
Pitkeathly, M.3
Baum, J.4
Dobson, C.M.5
-
26
-
-
0027308278
-
Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach
-
de Dios, A.C., Pearson, J.G. & Oldfield, E. Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. Science 260, 1491-1496 (1993).
-
(1993)
Science
, vol.260
, pp. 1491-1496
-
-
De Dios, A.C.1
Pearson, J.G.2
Oldfield, E.3
-
27
-
-
0347610773
-
Empirical correlation between protein backbone conformation and Cα and Cβ 13C nuclear magnetic resonance chemical shifts
-
Spera, S. & Bax, A. Empirical correlation between protein backbone conformation and Cα and Cβ 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113, 5490-5492 (1991).
-
(1991)
J. Am. Chem. Soc.
, vol.113
, pp. 5490-5492
-
-
Spera, S.1
Bax, A.2
-
28
-
-
0028393784
-
The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
-
Wishart, D.S. & Sykes, B.D. The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180 (1994).
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 171-180
-
-
Wishart, D.S.1
Sykes, B.D.2
-
29
-
-
0029181728
-
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids: I. Investigations of nearest neighbor effects
-
Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S. & Sykes, B.D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids: I. Investigations of nearest neighbor effects. J. Biomol. NMR 5, 67-81 (1995).
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 67-81
-
-
Wishart, D.S.1
Bigam, C.G.2
Holm, A.3
Hodges, R.S.4
Sykes, B.D.5
-
30
-
-
0021764802
-
Polypeptide secondary structure determination by nuclear magnetic resonance observation of short protonproton distances
-
Wüthrich, K., Billeter, M. & Braun, W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short protonproton distances. J. Mol. Biol. 180, 715-740 (1984).
-
(1984)
J. Mol. Biol.
, vol.180
, pp. 715-740
-
-
Wüthrich, K.1
Billeter, M.2
Braun, W.3
-
31
-
-
0027165688
-
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- And H-helices of myoglobin
-
Waltho, J.P., Feher, V.A., Merutka, G., Dyson, H.J. & Wright, P.E. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry 32, 6337-6347 (1993).
-
(1993)
Biochemistry
, vol.32
, pp. 6337-6347
-
-
Waltho, J.P.1
Feher, V.A.2
Merutka, G.3
Dyson, H.J.4
Wright, P.E.5
-
32
-
-
0023042853
-
X-ray structure and refinement of carbon-monoxy (Fe ll)-myoglobin at 1.5 Å resolution
-
Kuriyan, J., Wilz, S., Karplus, M. & Petsko, G,A. X-ray structure and refinement of carbon-monoxy (Fe ll)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 192, 133-154 (1986).
-
(1986)
J. Mol. Biol.
, vol.192
, pp. 133-154
-
-
Kuriyan, J.1
Wilz, S.2
Karplus, M.3
Petsko, G.A.4
-
33
-
-
0030947929
-
Folding propensities of peptide fragments of myoglobin
-
Reymond, M.T., Merutka, G., Dyson, H.J. & Wright, P.E. Folding propensities of peptide fragments of myoglobin. Prot Sci. 6, 706-716 (1997).
-
(1997)
Prot Sci.
, vol.6
, pp. 706-716
-
-
Reymond, M.T.1
Merutka, G.2
Dyson, H.J.3
Wright, P.E.4
-
34
-
-
0020475449
-
A simple method for displaying the hydropathic character of a protein
-
Kyte, J. & Doolittle, R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132 (1982).
-
(1982)
J. Mol. Biol.
, vol.157
, pp. 105-132
-
-
Kyte, J.1
Doolittle, R.F.2
-
35
-
-
0027988297
-
Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease
-
Alexandrescu, A.T. & Shortle, D. Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease. J. Mol. Biol. 242, 527-546 (1994).
-
(1994)
J. Mol. Biol.
, vol.242
, pp. 527-546
-
-
Alexandrescu, A.T.1
Shortle, D.2
-
36
-
-
5244224827
-
X-ray and NMR structure of human BCI-XL, an inhibitor of programmed cell death
-
Muchmore, S.W. et al. X-ray and NMR structure of human BCI-XL, an inhibitor of programmed cell death. Nature 381, 335-341 (1996).
-
(1996)
Nature
, vol.381
, pp. 335-341
-
-
Muchmore, S.W.1
-
37
-
-
0028466393
-
Molten globular characteristics of the native state of apomyoglobin
-
Un, L., Pinker, R.J., Forde, K., Rose, G.D. & Kallenbach, N.R. Molten globular characteristics of the native state of apomyoglobin. Nature Struct. Biol. 1, 447-452 (1994).
-
(1994)
Nature Struct. Biol.
, vol.1
, pp. 447-452
-
-
Un, L.1
Pinker, R.J.2
Forde, K.3
Rose, G.D.4
Kallenbach, N.R.5
-
38
-
-
0031581883
-
Probing the conformational state of apomyoglobin by limited proteolysis
-
Fontana, A. et al. Probing the conformational state of apomyoglobin by limited proteolysis. J. Mol. Biol. 266, 223-230 (1997).
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 223-230
-
-
Fontana, A.1
-
39
-
-
0029973119
-
Direct observation of fast protein folding: The initial collapse of apomyoglobin
-
Ballew, R.M., Sabelko, J. & Gruebele, M. Direct observation of fast protein folding: The initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. USA 93, 5759-5764 (1996).
-
(1996)
Proc. Natl. Acad. Sci. USA
, vol.93
, pp. 5759-5764
-
-
Ballew, R.M.1
Sabelko, J.2
Gruebele, M.3
-
40
-
-
0029858841
-
Observation of distinct nanosecond and microsecond protein folding events
-
Ballew, R.M., Sabelko, J. & Gruebele, M. Observation of distinct nanosecond and microsecond protein folding events. Nature Struct. Biol. 3, 923-926 (1996).
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 923-926
-
-
Ballew, R.M.1
Sabelko, J.2
Gruebele, M.3
-
41
-
-
0025150383
-
Origins of structure in globular proteins
-
Chan, H.S. & Dill, K.A. Origins of structure in globular proteins. Proc. Natl. Acad. Sci. USA 87, 6388-6392 (1990).
-
(1990)
Proc. Natl. Acad. Sci. USA
, vol.87
, pp. 6388-6392
-
-
Chan, H.S.1
Dill, K.A.2
-
42
-
-
0029032691
-
Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
-
Kataoka, M. et al. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol, 249, 215-228 (1995).
-
(1995)
J. Mol. Biol
, vol.249
, pp. 215-228
-
-
Kataoka, M.1
-
43
-
-
0015870378
-
Circular dichroism and optical rotatory dispersion of proteins and polypeptides
-
Adler, A.J., Greenfield, N.J. & Fasman, G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Meth. Enz. 27, 675-735 (1973).
-
(1973)
Meth. Enz.
, vol.27
, pp. 675-735
-
-
Adler, A.J.1
Greenfield, N.J.2
Fasman, G.D.3
-
44
-
-
0024278572
-
Folding of immunogenic peptide fragments of proteins in water solution. II the nascent helix
-
Dyson, H.J., Ranee, M., Houghten, R.A., Wright P.E. & Lerner, R.A. Folding of immunogenic peptide fragments of proteins in water solution. II The nascent helix- J. Mol. Biol. 201, 201-217 (1988).
-
(1988)
J. Mol. Biol.
, vol.201
, pp. 201-217
-
-
Dyson, H.J.1
Ranee, M.2
Houghten, R.A.3
Wright, P.E.4
Lerner, R.A.5
-
45
-
-
0027245421
-
Three-state analysis of sperm whale apomyoglobin folding
-
Barrick, D. & Baldwin, R.L Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 32, 3790-3796 (1993).
-
(1993)
Biochemistry
, vol.32
, pp. 3790-3796
-
-
Barrick, D.1
Baldwin, R.L.2
-
46
-
-
0028061408
-
Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
-
Gast, K. et al. Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate. Eur. Biophys. J. 23, 297-305 (1994).
-
(1994)
Eur. Biophys. J.
, vol.23
, pp. 297-305
-
-
Gast, K.1
-
47
-
-
0025891257
-
Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
-
Hughson, P.M., Barrick, D. & Baldwin, R.L, Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry 30, 4113-4118 (1991).
-
(1991)
Biochemistry
, vol.30
, pp. 4113-4118
-
-
Hughson, P.M.1
Barrick, D.2
Baldwin, R.L.3
-
48
-
-
0029981924
-
Packing interactions in the apomyoglobin folding intermediate
-
Kay, M.S. & Baldwin, R.L. Packing interactions in the apomyoglobin folding intermediate. Nature Struct. Biol. 3, 439-445 (1996).
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 439-445
-
-
Kay, M.S.1
Baldwin, R.L.2
-
49
-
-
0030737873
-
Detection of residue contacts in a protein folding intermediate
-
Balbach, J. et al. Detection of residue contacts in a protein folding intermediate, Proc Natl. Acad. Sci. USA 94, 7182-7185 (1997).
-
(1997)
Proc Natl. Acad. Sci. USA
, vol.94
, pp. 7182-7185
-
-
Balbach, J.1
-
50
-
-
44949291986
-
Three-dimensional triple-resonance NMR spectroscopy of isotopicaiiy enriched proteins
-
Kay, L.E., Ikura, M., Tschudin, R. & Bax, A. Three-dimensional triple-resonance NMR spectroscopy of isotopicaiiy enriched proteins. J. Magn. Reson. 89, 496-514 (1990).
-
(1990)
J. Magn. Reson.
, vol.89
, pp. 496-514
-
-
Kay, L.E.1
Ikura, M.2
Tschudin, R.3
Bax, A.4
-
51
-
-
0026158667
-
An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the α-carbon of the preceding residue in uniformly 15N/13C enriched proteins
-
Bax, A. & Ikura, M. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the α-carbon of the preceding residue in uniformly 15N/13C enriched proteins. J. Biomol. NMR 1, 99-104 (1991).
-
(1991)
J. Biomol. NMR
, vol.1
, pp. 99-104
-
-
Bax, A.1
Ikura, M.2
-
52
-
-
43949167657
-
HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- And betacarbon resonances in proteins
-
Wittekind, M. & Mueller, L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and betacarbon resonances in proteins. J. Magn. Reson. 101, 201-205 (1993).
-
(1993)
J. Magn. Reson.
, vol.101
, pp. 201-205
-
-
Wittekind, M.1
Mueller, L.2
-
53
-
-
9444245493
-
Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
-
Grzesiek, S. & Bax, A. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293 (1992).
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 6291-6293
-
-
Grzesiek, S.1
Bax, A.2
-
54
-
-
0027569483
-
Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
-
Grzesiek, S. & Bax, A. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J. Biomol. NMR 3, 185-204 (1993).
-
(1993)
J. Biomol. NMR
, vol.3
, pp. 185-204
-
-
Grzesiek, S.1
Bax, A.2
-
55
-
-
0001436130
-
A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins
-
Lohr, F. & Ruterjans, H. A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins. J. Biomol. NMR 6, 189-197 (1995).
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 189-197
-
-
Lohr, F.1
Ruterjans, H.2
-
56
-
-
0028282555
-
Backbone dynamics of a free and a phosphopeptide- Complexed Src homology 2 domain studied by 15N NMR relaxation
-
Farrow, N.A. et al. Backbone dynamics of a free and a phosphopeptide- complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33, 5984-6003 (1994).
-
(1994)
Biochemistry
, vol.33
, pp. 5984-6003
-
-
Farrow, N.A.1
-
57
-
-
0029795404
-
High resolution crystal structures of the deoxy, oxy and aquomet forms of cobalt myoglobin
-
Brucker, E.A., Olson, J.S., Phillips, G.N., Jr., Dou, Y & Ikeda-Saito, M. High resolution crystal structures of the deoxy, oxy and aquomet forms of cobalt myoglobin. J. Biol. Chem. 271, 25419-25422 (1996).
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 25419-25422
-
-
Brucker, E.A.1
Olson, J.S.2
Phillips Jr., G.N.3
Dou, Y.4
Ikeda-Saito, M.5
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