-
1
-
-
0025019350
-
Conformational stability of globular proteins
-
Pace, C.N. (1990). Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17.
-
(1990)
Trends Biochem. Sci.
, vol.15
, pp. 14-17
-
-
Pace, C.N.1
-
2
-
-
0028929556
-
Principles of protein folding - A perspective from simple exact model
-
Dill, K.A., et al., & Chan, H.S. (1995). Principles of protein folding - a perspective from simple exact model. Protein Sei. 4, 561-602.
-
(1995)
Protein Sei.
, vol.4
, pp. 561-602
-
-
Dill, K.A.1
Chan, H.S.2
-
3
-
-
0027349239
-
Hydration and heat stability effects on protein unfolding
-
Oobatake, M. & Ooi, T. (1993). Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59, 237-284.
-
(1993)
Prog. Biophys. Mol. Biol.
, vol.59
, pp. 237-284
-
-
Oobatake, M.1
Ooi, T.2
-
5
-
-
0000697562
-
Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
-
Tanford, C., Kawahara, K. & Lapanje, S. (1967). Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J. Am. Chem. Soc. 89, 729-736.
-
(1967)
J. Am. Chem. Soc.
, vol.89
, pp. 729-736
-
-
Tanford, C.1
Kawahara, K.2
Lapanje, S.3
-
6
-
-
0014199111
-
Evidence for residual structure in acid- And heat-denatured proteins
-
Aune, K.C., Salahuddin, A., Zarlengo, M.H. & Tanford, C. (1967). Evidence for residual structure in acid- and heat-denatured proteins. J. Biol. Chem. 242, 4486-4489.
-
(1967)
J. Biol. Chem.
, vol.242
, pp. 4486-4489
-
-
Aune, K.C.1
Salahuddin, A.2
Zarlengo, M.H.3
Tanford, C.4
-
7
-
-
0017042362
-
Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy
-
Nicoli, D.F. & Benedek, G.B. (1976). Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy. B/opolymers 15, 2421-2437.
-
(1976)
B/opolymers
, vol.15
, pp. 2421-2437
-
-
Nicoli, D.F.1
Benedek, G.B.2
-
8
-
-
0019944760
-
Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism
-
Labhardt, A.M. (1982). Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism. J. Mot. Biol. 157, 331-355.
-
(1982)
J. Mot. Biol.
, vol.157
, pp. 331-355
-
-
Labhardt, A.M.1
-
9
-
-
0025999787
-
Hydrogen exchange in thermally denatured ribonuclease A
-
Robertson, A.D. & Baldwin, R.L (1991). Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry 30, 9907-9914.
-
(1991)
Biochemistry
, vol.30
, pp. 9907-9914
-
-
Robertson, A.D.1
Baldwin, R.L.2
-
10
-
-
0026733250
-
Denatured states of ribonuclease A have compact dimensions and residual secondary structure
-
Sosnick, T.R. & Trewhella, J. (1992). Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry 31, 8329-8355.
-
(1992)
Biochemistry
, vol.31
, pp. 8329-8355
-
-
Sosnick, T.R.1
Trewhella, J.2
-
11
-
-
0028349385
-
Thermally denatured ribonuclease A retains secondary structure as shown by FTIR
-
Seshadri, S., Oberg, K.A. & Fink, A.L. (1994). Thermally denatured ribonuclease A retains secondary structure as shown by FTIR. Biochemistry 33, 1351-1355.
-
(1994)
Biochemistry
, vol.33
, pp. 1351-1355
-
-
Seshadri, S.1
Oberg, K.A.2
Fink, A.L.3
-
12
-
-
0028925816
-
Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
-
Tamura, Y. & Gekko, K. (1995). Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility. Biochemistry 34, 1878-1884.
-
(1995)
Biochemistry
, vol.34
, pp. 1878-1884
-
-
Tamura, Y.1
Gekko, K.2
-
13
-
-
0027394285
-
Pulsed H/D-exchange studies of folding intermediates
-
Baldwin, R.L. (1993). Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3, 84-91.
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 84-91
-
-
Baldwin, R.L.1
-
14
-
-
0027955639
-
Small angle X-ray scattering studies of protein folding
-
Lattman, E.E. (1994). Small angle X-ray scattering studies of protein folding. Curr. Opin. Struct. Biol. 4, 87-92.
-
(1994)
Curr. Opin. Struct. Biol.
, vol.4
, pp. 87-92
-
-
Lattman, E.E.1
-
15
-
-
0030324821
-
X-ray solution scattering studies of protein folding
-
Kataoka, M. & Goto, Y. (1996). X-ray solution scattering studies of protein folding. Fold Des. 1, R107-R114.
-
(1996)
Fold Des.
, vol.1
-
-
Kataoka, M.1
Goto, Y.2
-
16
-
-
0017701604
-
Automatic identification of secondary structure in globular proteins
-
Levitt, M. & Greer, J. (1977). Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114, 181-239.
-
(1977)
J. Mol. Biol.
, vol.114
, pp. 181-239
-
-
Levitt, M.1
Greer, J.2
-
17
-
-
0019888571
-
Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure
-
Takano, T. & Dickerson, R.E. (1981). Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure. J. Mol. Biol. 153, 95-115.
-
(1981)
J. Mol. Biol.
, vol.153
, pp. 95-115
-
-
Takano, T.1
Dickerson, R.E.2
-
18
-
-
0027400842
-
Molten globule of cytochrome c studied by small angle X-ray scattering
-
Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229, 591-596.
-
(1993)
J. Mol. Biol.
, vol.229
, pp. 591-596
-
-
Kataoka, M.1
Hagihara, Y.2
Mihara, K.3
Goto, Y.4
-
19
-
-
0029040449
-
Thermodynamic stability of the molten globule states of apomyoglobin
-
Nishii, I., Kataoka, M. & Goto, Y. (1995). Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250, 223-238.
-
(1995)
J. Mol. Biol.
, vol.250
, pp. 223-238
-
-
Nishii, I.1
Kataoka, M.2
Goto, Y.3
-
20
-
-
0029032691
-
Structural characterization of molten globule and native states of apomyoglobin by solution X-ray scattering
-
Kataoka, M., et al., & Goto, Y. (1995). Structural characterization of molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249, 215-228.
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 215-228
-
-
Kataoka, M.1
Goto, Y.2
-
21
-
-
0031050429
-
Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering
-
Kataoka, M., Kuwajima, K., Tokunaga, F. & Goto, Y. (1997). Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering. Protein Sci. 6, 422-430.
-
(1997)
Protein Sci.
, vol.6
, pp. 422-430
-
-
Kataoka, M.1
Kuwajima, K.2
Tokunaga, F.3
Goto, Y.4
-
22
-
-
0027184188
-
Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast
-
Damaschun, G., et al., & Zirwer, D. (1993). Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. Biochemistry 32, 7739-7746.
-
(1993)
Biochemistry
, vol.32
, pp. 7739-7746
-
-
Damaschun, G.1
Zirwer, D.2
-
23
-
-
0030572626
-
A lysozyme folding intermediate revealed by solution X-ray scattering
-
Chen, L., Hodgson, K.O. & Doniach, S..(1996). A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261, 658-671.
-
(1996)
J. Mol. Biol.
, vol.261
, pp. 658-671
-
-
Chen, L.1
Hodgson, K.O.2
Doniach, S.3
-
24
-
-
0025299563
-
Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. the mean-square of the end-to-end distance and of the dipole moment
-
Rowe, G. & Pineiro, A.L. (1990). Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. The mean-square of the end-to-end distance and of the dipole moment. Biophys. Chem. 36, 57-64.
-
(1990)
Biophys. Chem.
, vol.36
, pp. 57-64
-
-
Rowe, G.1
Pineiro, A.L.2
-
25
-
-
0028978422
-
Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
-
Shiraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-184.
-
(1995)
J. Mol. Biol.
, vol.245
, pp. 180-184
-
-
Shiraki, K.1
Nishikawa, K.2
Goto, Y.3
-
26
-
-
0029893286
-
The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD, fluorescence, NMR and small angle X-ray scattering
-
Kamatari, Y.O., Konno, T., Kataoka, M. & Akasaka, K. (1996). The methanol-induced globular and expanded denatured states of cytochrome c: a study by CD, fluorescence, NMR and small angle X-ray scattering. J. Mol. Biol. 259, 512-523.
-
(1996)
J. Mol. Biol.
, vol.259
, pp. 512-523
-
-
Kamatari, Y.O.1
Konno, T.2
Kataoka, M.3
Akasaka, K.4
-
27
-
-
0029967685
-
15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol
-
15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. J. Mol. Biol. 257, 669-683.
-
(1996)
J. Mol. Biol.
, vol.257
, pp. 669-683
-
-
Buck, M.1
Schwalbe, H.2
Dobson, C.M.3
-
28
-
-
0030828611
-
Trifluoroethanol-induced conformational transition of hen eggwhite lysozyme studied by small-angle X-ray scattering
-
Hoshino, M., Hagihara, Y., Hamada, D., Kataoka, M. & Goto, Y. (1997). Trifluoroethanol-induced conformational transition of hen eggwhite lysozyme studied by small-angle X-ray scattering. FEBS Lett. 416, 72-76.
-
(1997)
FEBS Lett.
, vol.416
, pp. 72-76
-
-
Hoshino, M.1
Hagihara, Y.2
Hamada, D.3
Kataoka, M.4
Goto, Y.5
-
29
-
-
33845555570
-
Titration of individual components in a mixture with resolution of difference spectra, pKs and redox transitions
-
Shrager, R.I. & Hendler, R.W. (1982). Titration of individual components in a mixture with resolution of difference spectra, pKs and redox transitions. Anal. Chem. 54, 1147-1152.
-
(1982)
Anal. Chem.
, vol.54
, pp. 1147-1152
-
-
Shrager, R.I.1
Hendler, R.W.2
-
30
-
-
0030320442
-
The concept of a random coil. Residual structure in peptides and denatured proteins
-
Smith, L.J., Fiebig, K.M., Schwalbe, H. & Dobson, C.M. (1996). The concept of a random coil. Residual structure in peptides and denatured proteins. Fold. Des. 1, R95-R106.
-
(1996)
Fold. Des.
, vol.1
-
-
Smith, L.J.1
Fiebig, K.M.2
Schwalbe, H.3
Dobson, C.M.4
-
31
-
-
0029978353
-
Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and denatured conformations
-
Smith, L.J., et al., & Dobson, C.M. (1996). Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and denatured conformations. J. Mol. Biol. 255, 494-506.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 494-506
-
-
Smith, L.J.1
Dobson, C.M.2
-
32
-
-
0000749460
-
Towards a description of the conformation 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. (1996). Towards a description of the conformation of denatured states of proteins. Comparison of a random coil model with NMR measurements. J. Phys. Chem. 100, 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
-
33
-
-
0029961647
-
Structural analysis of non-native states of proteins by NMR
-
Shortle, D.R. (1996). Structural analysis of non-native states of proteins by NMR. Curr. Opin. Struct. Biol. 6, 24-30.
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 24-30
-
-
Shortle, D.R.1
-
34
-
-
0030032461
-
The denatured state (the other half of the folding equation) and its role in protein stability
-
Shortle, D.R. (1996). 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.R.1
-
35
-
-
0006555359
-
Structural studies of ribonuclease. XI. Kinetics of denaturation
-
Scott, R.A. & Scheraga, H.A. (1963). Structural studies of ribonuclease. XI. Kinetics of denaturation. J. Am. Chem. Soc. 85, 3866-3873.
-
(1963)
J. Am. Chem. Soc.
, vol.85
, pp. 3866-3873
-
-
Scott, R.A.1
Scheraga, H.A.2
-
36
-
-
0015526732
-
Participation of the protein ligands in the folding of cytochrome c
-
Babul, J. & Stellwagen, E. (1972). Participation of the protein ligands in the folding of cytochrome c. Biochemistry 11, 1195-1200.
-
(1972)
Biochemistry
, vol.11
, pp. 1195-1200
-
-
Babul, J.1
Stellwagen, E.2
-
37
-
-
0022160183
-
Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation
-
Ueki, T., er al., & Muroga, Y. (1985). Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation. Biophys. Chem. 23, 115-124.
-
(1985)
Biophys. Chem.
, vol.23
, pp. 115-124
-
-
Ueki, T.1
Muroga, Y.2
-
39
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
-
(1991)
J. Appl. Crystallogr.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
40
-
-
0028057108
-
Raster3D version 2.0. A program for photorealistic molecular graphics
-
Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
-
(1994)
Acta Crystallogr. D
, vol.50
, pp. 869-873
-
-
Merritt, E.A.1
Murphy, M.E.P.2
|