-
1
-
-
0030032461
-
The denatured state (the other half of the folding equation) and its role in protein stability
-
Shortle, D. (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.1
-
2
-
-
0027918159
-
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease
-
Shortle, D. & Abeygunawardana, C. (1993). NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure 1, 121-134.
-
(1993)
Structure
, vol.1
, pp. 121-134
-
-
Shortle, D.1
Abeygunawardana, C.2
-
3
-
-
0028866620
-
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin
-
Schulman, B.A., Redfield, C., Peng, Z.-Y., Dobson, C.M. & Kim, P.S. (1995). Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J. Mol. Biol. 253, 651-657.
-
(1995)
J. Mol. Biol.
, vol.253
, pp. 651-657
-
-
Schulman, B.A.1
Redfield, C.2
Peng, Z.-Y.3
Dobson, C.M.4
Kim, P.S.5
-
4
-
-
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
-
5
-
-
0028929556
-
Principles of protein folding - A perspective from simple exact models
-
Dill. K.A., et al., & Chan, H.S. (1995). Principles of protein folding - a perspective from simple exact models. Protein Sci. 4, 561-602.
-
(1995)
Protein Sci.
, vol.4
, pp. 561-602
-
-
Dill, K.A.1
Chan, H.S.2
-
6
-
-
0027955639
-
Small angle scattering studies of protein folding
-
Lattman, E.E. (1994). Small angle 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
-
7
-
-
0028224689
-
Modeling compact denatured states of proteins
-
Lattman, E.E., Fiebig, K.M. & Dill, K.A. (1994). Modeling compact denatured states of proteins. Biochemistry 33, 6158-6166.
-
(1994)
Biochemistry
, vol.33
, pp. 6158-6166
-
-
Lattman, E.E.1
Fiebig, K.M.2
Dill, K.A.3
-
8
-
-
0027400842
-
Molten globule of cytochrome c studied by the small angle X-ray scattering
-
Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by the 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
-
9
-
-
0001885952
-
Use of X-ray solution scattering for protein folding study
-
(Chance, B., et al., eds.), Clarendon Press, Oxford
-
Kataoka, M., Flanagan, J.M., Tokunaga, F. & Engelman, D.M. (1994). Use of X-ray solution scattering for protein folding study. In Synchrotron Radiation in Biosciences. (Chance, B., et al., eds.), pp. 187-194, Clarendon Press, Oxford.
-
(1994)
Synchrotron Radiation in Biosciences
, pp. 187-194
-
-
Kataoka, M.1
Flanagan, J.M.2
Tokunaga, F.3
Engelman, D.M.4
-
10
-
-
0029032691
-
Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
-
Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F. & Goto, Y. (1995). Structural characterization of the 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
Nishii, I.2
Fujisawa, T.3
Ueki, T.4
Tokunaga, F.5
Goto, Y.6
-
11
-
-
0027337984
-
Configurational distribution of denatured phosphoglycerate kinase
-
Calmettes, P., Roux, B., Durand, D., Desmadril, M. & Smith, J.C. (1993). Configurational distribution of denatured phosphoglycerate kinase. J. Mol. Biol. 231, 840-848.
-
(1993)
J. Mol. Biol.
, vol.231
, pp. 840-848
-
-
Calmettes, P.1
Roux, B.2
Durand, D.3
Desmadril, M.4
Smith, J.C.5
-
12
-
-
0028173333
-
How random is a highly denatured protein?
-
Calmettes, P., Durand, D., Desmadril, M., Minard, P., Receveur, V. & Smith, J.C. (1994). How random is a highly denatured protein? Biophys. Chem. 53, 105-114.
-
(1994)
Biophys. Chem.
, vol.53
, pp. 105-114
-
-
Calmettes, P.1
Durand, D.2
Desmadril, M.3
Minard, P.4
Receveur, V.5
Smith, J.C.6
-
13
-
-
0025732606
-
Acid denatured apo-cytochrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering
-
Damaschun, G., Damaschun, H., Gast, K., Gernat, C. & Zirwer, D. (1991). Acid denatured apo-cytochrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering. Biochim. Biophys. Acta 1078, 289-295.
-
(1991)
Biochim. Biophys. Acta
, vol.1078
, pp. 289-295
-
-
Damaschun, G.1
Damaschun, H.2
Gast, K.3
Gernat, C.4
Zirwer, D.5
-
14
-
-
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
-
15
-
-
0028061408
-
Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
-
Gast, K., Damaschun, H., Misselwitz, R., Muller-Frohne, M., Zirwer, D. & Damaschun, G. (1994). Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate. Eur. Biophys. J. 23, 297-305.
-
(1994)
Eur. Biophys. J.
, vol.23
, pp. 297-305
-
-
Gast, K.1
Damaschun, H.2
Misselwitz, R.3
Muller-Frohne, M.4
Zirwer, D.5
Damaschun, G.6
-
16
-
-
0026543378
-
Truncated staphylococcal nuclease is compact but disordered
-
Flanagan, J.M., Kataoka, M., Shortle, D. & Engelman, D.M. (1992). Truncated staphylococcal nuclease is compact but disordered. Proc. Natl. Acad. Sci. USA 89, 748-752.
-
(1992)
Proc. Natl. Acad. Sci. USA
, vol.89
, pp. 748-752
-
-
Flanagan, J.M.1
Kataoka, M.2
Shortle, D.3
Engelman, D.M.4
-
17
-
-
0027495402
-
Mutation can cause large changes in the conformation of a denatured protein
-
Flanagan, J.M., Kataoka, M., Fujisawa, T. & Engelman, D.M. (1993). Mutation can cause large changes in the conformation of a denatured protein. Biochemistry 32, 10359-10370.
-
(1993)
Biochemistry
, vol.32
, pp. 10359-10370
-
-
Flanagan, J.M.1
Kataoka, M.2
Fujisawa, T.3
Engelman, D.M.4
-
18
-
-
0029126840
-
Solution X-ray scattering analysis of cold- Heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor
-
Konno, T., Kataoka, M., Kamatari, Y., Kanaori, K., Nosaka, A. & Akasaka, K. (1995). Solution X-ray scattering analysis of cold- heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor. J. Mol. Biol. 251, 95-103.
-
(1995)
J. Mol. Biol.
, vol.251
, pp. 95-103
-
-
Konno, T.1
Kataoka, M.2
Kamatari, Y.3
Kanaori, K.4
Nosaka, A.5
Akasaka, K.6
-
19
-
-
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., 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.1
Konno, T.2
Kataoka, M.3
Akasaka, K.4
-
20
-
-
0027301270
-
Evidence of an associative intermediate on the myoglobin refolding pathway
-
Eliezer, D., Chiba, K., Tsuruta, H., Doniach, S., Hodgson, K.O. & Kihara, H. (1993). Evidence of an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65, 912-917.
-
(1993)
Biophys. J.
, vol.65
, pp. 912-917
-
-
Eliezer, D.1
Chiba, K.2
Tsuruta, H.3
Doniach, S.4
Hodgson, K.O.5
Kihara, H.6
-
21
-
-
0028884580
-
The radius of gyration of an apomyoglobin folding intermediate
-
Eliezer, D., Jennings, P.A., Wright, P.E., Doniach, S., Hodgson, K.O. & Tsuruta, H. (1995). The radius of gyration of an apomyoglobin folding intermediate. Science 270, 487-488.
-
(1995)
Science
, vol.270
, pp. 487-488
-
-
Eliezer, D.1
Jennings, P.A.2
Wright, P.E.3
Doniach, S.4
Hodgson, K.O.5
Tsuruta, H.6
-
22
-
-
0030569018
-
Protein globularization during folding. a study by synchrotron small-angle X-ray scattering
-
in press
-
Semisotnov, G.V., et al., & Kuwajima, K. (1996). Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J. Mol. Biol. in press.
-
(1996)
J. Mol. Biol.
-
-
Semisotnov, G.V.1
Kuwajima, K.2
-
25
-
-
36949091243
-
Structure of myoglobin - Three dimensional Fourier synthesis at 2 Å resolution
-
Kendrew, J.C., et al., & Shore, V.C. (1960). Structure of myoglobin - three dimensional Fourier synthesis at 2 Å resolution. Nature 185, 422-427.
-
(1960)
Nature
, vol.185
, pp. 422-427
-
-
Kendrew, J.C.1
Shore, V.C.2
-
26
-
-
84985665860
-
On the interpretation and prediction of X-ray scattering profiles of biomolecules in solution
-
Pickover, C.A. & Engelman, D.M. (1981). On the interpretation and prediction of X-ray scattering profiles of biomolecules in solution. Biopolymers 21, 817-831.
-
(1981)
Biopolymers
, vol.21
, pp. 817-831
-
-
Pickover, C.A.1
Engelman, D.M.2
-
27
-
-
0024485714
-
Rapid calculation of the solution scattering profile from a macromolecule of known structure
-
Lattman, E.E. (1989). Rapid calculation of the solution scattering profile from a macromolecule of known structure. Proteins 5, 149-155.
-
(1989)
Proteins
, vol.5
, pp. 149-155
-
-
Lattman, E.E.1
-
28
-
-
0014364651
-
Protein denaturation
-
Tanford, C. (1968). Protein denaturation. Adv. Protein Chem. 23, 121-275.
-
(1968)
Adv. Protein Chem.
, vol.23
, pp. 121-275
-
-
Tanford, C.1
-
29
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103.
-
(1989)
Proteins
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
30
-
-
0002940127
-
The molten globule state
-
(Creighton, E.E., ed.), WH Freeman and Co, New York
-
Ptitsyn, O.B. (1992). The molten globule state. In Protein Folding. (Creighton, E.E., ed.), pp. 243-400, WH Freeman and Co, New York.
-
(1992)
Protein Folding
, pp. 243-400
-
-
Ptitsyn, O.B.1
-
31
-
-
0029157429
-
Compact intermediate states in protein folding
-
Fink, A.L. (1995). Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
-
(1995)
Annu. Rev. Biophys. Biomol. Struct.
, vol.24
, pp. 495-522
-
-
Fink, A.L.1
-
32
-
-
0028402689
-
The barriers in protein folding
-
Sosnick, T.R., Mayne, L., Hiller, R. & Englander, S.W. (1994). The barriers in protein folding. Nat Struct. Biol. 1, 149-156.
-
(1994)
Nat Struct. Biol.
, vol.1
, pp. 149-156
-
-
Sosnick, T.R.1
Mayne, L.2
Hiller, R.3
Englander, S.W.4
-
33
-
-
0028856785
-
Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
-
Fersht, A.R. (1995). Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA 92, 10869-10873.
-
(1995)
Proc. Natl. Acad. Sci. USA
, vol.92
, pp. 10869-10873
-
-
Fersht, A.R.1
-
34
-
-
0028243107
-
Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
-
Nishii, I., Kataoka, M., Tokunaga, F. & Goto, Y. (1994). Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 33, 4903-4909.
-
(1994)
Biochemistry
, vol.33
, pp. 4903-4909
-
-
Nishii, I.1
Kataoka, M.2
Tokunaga, F.3
Goto, Y.4
-
35
-
-
0029863253
-
Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c
-
Hamada, D., Kuroda, Y., Kataoka, M., Aimoto, S., Yoshimura, T. & Goto, Y. (1996). Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
-
(1996)
J. Mol. Biol.
, vol.256
, pp. 172-186
-
-
Hamada, D.1
Kuroda, Y.2
Kataoka, M.3
Aimoto, S.4
Yoshimura, T.5
Goto, Y.6
-
36
-
-
0019890466
-
α-Lactalbumin: Compact state with fluctuating tertiary structure?
-
Dolgikh, D.A., et al., & Ptitsyn, O.B. (1981). α-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett. 136, 311-315.
-
(1981)
FEBS Lett.
, vol.136
, pp. 311-315
-
-
Dolgikh, D.A.1
Ptitsyn, O.B.2
-
37
-
-
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, 8329-8335.
-
(1992)
Biochemistry
, vol.31
, pp. 8329-8335
-
-
Sosnick, T.R.1
Trewhella, J.2
-
38
-
-
0000739195
-
Melittin binding causes a large calcium-dependent conformational change in ćalmodulin
-
Kataoka, M., Head, J.F., Seaton, B.A. & Engelman, D.M. (1989). Melittin binding causes a large calcium-dependent conformational change in ćalmodulin. Proc. Natl. Acad. Sci. USA 86, 6944-6948.
-
(1989)
Proc. Natl. Acad. Sci. USA
, vol.86
, pp. 6944-6948
-
-
Kataoka, M.1
Head, J.F.2
Seaton, B.A.3
Engelman, D.M.4
-
39
-
-
0029014386
-
Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
-
Loh, S.N., Kay, M.S. & Baldwin, R.L. (1995). Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. USA 92, 5446-5450.
-
(1995)
Proc. Natl. Acad. Sci. USA
, vol.92
, pp. 5446-5450
-
-
Loh, S.N.1
Kay, M.S.2
Baldwin, R.L.3
-
40
-
-
0030010408
-
Intermediate states in protein folding
-
Privalov, P.L (1996). Intermediate states in protein folding. J. Mol. Biol. 258, 707-725.
-
(1996)
J. Mol. Biol.
, vol.258
, pp. 707-725
-
-
Privalov, P.L.1
|