-
1
-
-
0028009873
-
Characterization of a trifluoroethanol induced partially folded state of α-lactalbumin
-
Alexandrescu AT, Ng Y-L, Dobson CM. 1994. Characterization of a trifluoroethanol induced partially folded state of α-lactalbumin. J Mol Biol 235:587-599.
-
(1994)
J Mol Biol
, vol.235
, pp. 587-599
-
-
Alexandrescu, A.T.1
Ng, Y.-L.2
Dobson, C.M.3
-
2
-
-
0027254057
-
The molten globule intermediate of apomyoglobin and the process of protein folding
-
Barrick D, Baldwin RL. 1993. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci 2:869-876.
-
(1993)
Protein Sci
, vol.2
, pp. 869-876
-
-
Barrick, D.1
Baldwin, R.L.2
-
3
-
-
0014939906
-
The role of aliphatic alcohols on the stability of collagen and tropocollagen
-
Bianchi E, Rampone R, Tealdi A, Ciferri A. 1970. The role of aliphatic alcohols on the stability of collagen and tropocollagen. J Biol Chem 245:3341-3345.
-
(1970)
J Biol Chem
, vol.245
, pp. 3341-3345
-
-
Bianchi, E.1
Rampone, R.2
Tealdi, A.3
Ciferri, A.4
-
4
-
-
0028938267
-
Structural determinants of protein dynamics: Analysis of 15 N NMR relaxation measurements for main-chain and side chain nuclei of hen egg-white lysozyme
-
Buck M, Boyd J, Redfield C, MacKenzie DA, Jeenes DJ, Archer DB, Dobson CM. 1995a. Structural determinants of protein dynamics: Analysis of 15 N NMR relaxation measurements for main-chain and side chain nuclei of hen egg-white lysozyme. Biochemistry 34:4041-4055.
-
(1995)
Biochemistry
, vol.34
, pp. 4041-4055
-
-
Buck, M.1
Boyd, J.2
Redfield, C.3
MacKenzie, D.A.4
Jeenes, D.J.5
Archer, D.B.6
Dobson, C.M.7
-
5
-
-
0027492170
-
A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding
-
Buck M, Radford SE, Dobson CM. 1993. A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding. Biochemistry 32:667-678.
-
(1993)
Biochemistry
, vol.32
, pp. 667-678
-
-
Buck, M.1
Radford, S.E.2
Dobson, C.M.3
-
6
-
-
0028882136
-
Characterization of conformational preferences in a partially folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol
-
Buck M, Schwalbe H, Dobson CM. 1995b. Characterization of conformational preferences in a partially folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry 34:13219-13232.
-
(1995)
Biochemistry
, vol.34
, pp. 13219-13232
-
-
Buck, M.1
Schwalbe, H.2
Dobson, C.M.3
-
7
-
-
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
-
8
-
-
0029917563
-
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface
-
Bychkova VE, Dujsekina AE, Klenin SI, Tiktopulo EI, Uversky VN, Ptitsyn OB. 1996. Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35:6058-6063.
-
(1996)
Biochemistry
, vol.35
, pp. 6058-6063
-
-
Bychkova, V.E.1
Dujsekina, A.E.2
Klenin, S.I.3
Tiktopulo, E.I.4
Uversky, V.N.5
Ptitsyn, O.B.6
-
9
-
-
0025982146
-
Molten globule intermediates and protien folding
-
Chistensen H, Pain RH. 1991. Molten globule intermediates and protien folding. Eur Biophys J 19:221-229.
-
(1991)
Eur Biophys J
, vol.19
, pp. 221-229
-
-
Chistensen, H.1
Pain, R.H.2
-
10
-
-
0014939887
-
The effect of aliphatic alcohols on the helix-coil transition of poly-1-ornithine and poly-1-glutamic acid
-
Conio G, Patrone E, Brighetti S. 1970. The effect of aliphatic alcohols on the helix-coil transition of poly-1-ornithine and poly-1-glutamic acid. J Biol Chem 245:3335-3340.
-
(1970)
J Biol Chem
, vol.245
, pp. 3335-3340
-
-
Conio, G.1
Patrone, E.2
Brighetti, S.3
-
11
-
-
0026659508
-
Thermodynamics consequences of the removal of a disulphide bridge of hen lysozyme
-
Cooper A, Eyles SJ, Radford SE, Dobson CM. 1992. Thermodynamics consequences of the removal of a disulphide bridge of hen lysozyme. J Mol Biol 225:939-943.
-
(1992)
J Mol Biol
, vol.225
, pp. 939-943
-
-
Cooper, A.1
Eyles, S.J.2
Radford, S.E.3
Dobson, C.M.4
-
12
-
-
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
-
13
-
-
0027184188
-
Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast
-
Damaschun G, Damaschun H, Gast K, Misselwitz R, Muller JJ, Pfeil W, 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
Damaschun, H.2
Gast, K.3
Misselwitz, R.4
Muller, J.J.5
Pfeil, W.6
Zirwer, D.7
-
14
-
-
0001931668
-
Unfolded proteins, compact states and molten globules
-
Dobson CM. 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
-
15
-
-
0028053187
-
Understanding how proteins fold: The lysozyme story so far
-
Dobson CM, Evans PA, Redford SE. 1994. Understanding how proteins fold: The lysozyme story so far. TIBS 19:31-37.
-
(1994)
TIBS
, vol.19
, pp. 31-37
-
-
Dobson, C.M.1
Evans, P.A.2
Redford, S.E.3
-
16
-
-
0026768829
-
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
-
Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE. 1992a. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J Mol Biol 226:795-817.
-
(1992)
J Mol Biol
, vol.226
, pp. 795-817
-
-
Dyson, H.J.1
Merutka, G.2
Waltho, J.P.3
Lerner, R.A.4
Wright, P.E.5
-
17
-
-
0026743136
-
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Plastocyanin
-
Dyson HJ, Sayre JR, Merutka G, Shin HC, Lerner RA, Wright PE. 1992b. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Plastocyanin. J Mol Biol 226:819-835.
-
(1992)
J Mol Biol
, vol.226
, pp. 819-835
-
-
Dyson, H.J.1
Sayre, J.R.2
Merutka, G.3
Shin, H.C.4
Lerner, R.A.5
Wright, P.E.6
-
18
-
-
0023118118
-
Characterization of the unfolding of ribonuclease a in aqueous methanol solvent
-
Fink AL, Painter B. 1987. Characterization of the unfolding of ribonuclease A in aqueous methanol solvent. Biochemistry 26:1665-1671.
-
(1987)
Biochemistry
, vol.26
, pp. 1665-1671
-
-
Fink, A.L.1
Painter, B.2
-
19
-
-
0027495402
-
Mutation can cause large changes in the conformation of a denatured protein
-
Flanagan JM, Kataoka M, Fujisawa T, Engelman DM. 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
-
21
-
-
0022039517
-
Early stages in the trifluoroethanol-induced unfolding of hen egg-white lysozyme and its complex with (GlcNAc)3
-
Galat A. 1985. Early stages in the trifluoroethanol-induced unfolding of hen egg-white lysozyme and its complex with (GlcNAc)3. Biochem Biophys Acta 827:221-227.
-
(1985)
Biochem Biophys Acta
, vol.827
, pp. 221-227
-
-
Galat, A.1
-
23
-
-
0026351184
-
Role of electrostatic repulsion in the acid molten globule of cytochrome c
-
Goto Y, Nishikiori S. 1991. Role of electrostatic repulsion in the acid molten globule of cytochrome c. J Mol Biol 222:679-686.
-
(1991)
J Mol Biol
, vol.222
, pp. 679-686
-
-
Goto, Y.1
Nishikiori, S.2
-
24
-
-
0025195499
-
Mechanism of acid-induced folding of proteins
-
Goto Y, Takahashi N, Fink AL. 1990b. Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488.
-
(1990)
Biochemistry
, vol.29
, pp. 3480-3488
-
-
Goto, Y.1
Takahashi, N.2
Fink, A.L.3
-
26
-
-
0028918781
-
An equilibrium partially folded state of human lysozyme at low pH
-
Haezebrouck P, Joniau M, Dael HV, Hooke SD, Woodruff ND, Dobson CM. 1995. An equilibrium partially folded state of human lysozyme at low pH. J Mol Biol 246:382-387.
-
(1995)
J Mol Biol
, vol.246
, pp. 382-387
-
-
Haezebrouck, P.1
Joniau, M.2
Dael, H.V.3
Hooke, S.D.4
Woodruff, N.D.5
Dobson, C.M.6
-
27
-
-
0014962109
-
On the structural stability and solvent denaturation of proteins
-
Herskovits TT, Gadegbeku B, Jaillet H. 1970. On the structural stability and solvent denaturation of proteins. J Biol Chem 245:2588-2598.
-
(1970)
J Biol Chem
, vol.245
, pp. 2588-2598
-
-
Herskovits, T.T.1
Gadegbeku, B.2
Jaillet, H.3
-
28
-
-
0031042309
-
Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol
-
Hirota N, Mizuno K, Goto Y. 1997. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci 6:416-421.
-
(1997)
Protein Sci
, vol.6
, pp. 416-421
-
-
Hirota, N.1
Mizuno, K.2
Goto, Y.3
-
29
-
-
0023041667
-
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of a la and lysozyme
-
Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 1986. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of a LA and lysozyme. Biochemistry 5:6965-6972.
-
(1986)
Biochemistry
, vol.5
, pp. 6965-6972
-
-
Ikeguchi, M.1
Kuwajima, K.2
Mitani, M.3
Sugai, S.4
-
30
-
-
0026009213
-
Stable submolecular folding units in non-compact form of cytochrome c
-
Jeng MF, Englander SW. 1991. Stable submolecular folding units in non-compact form of cytochrome c. J Mol Biol 221:1045-1061.
-
(1991)
J Mol Biol
, vol.221
, pp. 1045-1061
-
-
Jeng, M.F.1
Englander, S.W.2
-
31
-
-
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 YO, 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
-
32
-
-
0001885952
-
Use of X-ray solution scattering for protein folding study
-
Chance B, Deisenhofer J, Ebashi S, Goodhead DT, Helliwell JR, Huxley HE, Iizuka T, Kirz J, Mitsui T, Rubenstein E, Sakabe N, Sasaki T, Schmahl G, Stuhrmann HB, Wuthrich K, Zaccai G, eds. Oxford: Clarendon Press
-
Kataoka M, Flanagan JM, Tokunaga F, Engelman DM. 1994. Use of X-ray solution scattering for protein folding study. In: Chance B, Deisenhofer J, Ebashi S, Goodhead DT, Helliwell JR, Huxley HE, Iizuka T, Kirz J, Mitsui T, Rubenstein E, Sakabe N, Sasaki T, Schmahl G, Stuhrmann HB, Wuthrich K, Zaccai G, eds. Synchrotron radiation in the biosciences. Oxford: Clarendon Press. pp 187-194.
-
(1994)
Synchrotron Radiation in the Biosciences
, pp. 187-194
-
-
Kataoka, M.1
Flanagan, J.M.2
Tokunaga, F.3
Engelman, D.M.4
-
33
-
-
0030324821
-
X-ray solution scattering studies of protein folding
-
Kataoka M, Goto Y. 1996. X-ray solution scattering studies of protein folding. Folding & Design 1:R107-R114.
-
(1996)
Folding & Design
, vol.1
-
-
Kataoka, M.1
Goto, Y.2
-
34
-
-
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
-
35
-
-
0025778565
-
Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly α-helical conformation
-
Kataoka M, Head JF, Persechini A, Kretsinger RH, Engelman DM. 1991. Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly α-helical conformation. Biochemistry 30:1188-1192.
-
(1991)
Biochemistry
, vol.30
, pp. 1188-1192
-
-
Kataoka, M.1
Head, J.F.2
Persechini, A.3
Kretsinger, R.H.4
Engelman, D.M.5
-
36
-
-
0000739195
-
Melittin binding causes a large calcium-dependent conformational change in calmodulin
-
Kataoka M, Head JF, Seaton BA, Engelman DM. 1989. Melittin binding causes a large calcium-dependent conformational change in calmodulin. 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
-
37
-
-
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
-
38
-
-
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 T. 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, T.6
-
41
-
-
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
-
42
-
-
0026525049
-
Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process
-
Kuroda Y, Kidokoro S, Wada A. 1992. Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process. J Mol Biol 223:1139-1153.
-
(1992)
J Mol Biol
, vol.223
, pp. 1139-1153
-
-
Kuroda, Y.1
Kidokoro, S.2
Wada, A.3
-
43
-
-
0024417964
-
The molten globule states as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima K. 1989. The molten globule states as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct Funct Genet 6:87-103.
-
(1989)
Proteins Struct Funct Genet
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
44
-
-
0026940839
-
Protein folding in vivo
-
Kuwajima K. 1992. Protein folding in vivo. Curr Opin Biotechnol 3:462-467.
-
(1992)
Curr Opin Biotechnol
, vol.3
, pp. 462-467
-
-
Kuwajima, K.1
-
45
-
-
0027955639
-
Small angle scattering studies of protein folding
-
Lattman EE. 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
-
46
-
-
0025300073
-
Peptide α-helicity in aqueous trifluoroethanol: Correlations with predicted α-helicity and the secondary structure of the corresponding regions of bovine growth hormone
-
Lehrman SR, Tuls JL, Lund M. 1990. Peptide α-helicity in aqueous trifluoroethanol: Correlations with predicted α-helicity and the secondary structure of the corresponding regions of bovine growth hormone. Biochemistry 29:5590-5596.
-
(1990)
Biochemistry
, vol.29
, pp. 5590-5596
-
-
Lehrman, S.R.1
Tuls, J.L.2
Lund, M.3
-
47
-
-
0025325351
-
The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate
-
Nakano T, Fink AL. 1990. The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate. J Biol Chem 265:12356-12362.
-
(1990)
J Biol Chem
, vol.265
, pp. 12356-12362
-
-
Nakano, T.1
Fink, A.L.2
-
48
-
-
0022804939
-
Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol
-
Nelson JW, Kallenbach NR. 1986. Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol. Proteins Struct Fund Genet 1:211-217.
-
(1986)
Proteins Struct Fund Genet
, vol.1
, pp. 211-217
-
-
Nelson, J.W.1
Kallenbach, N.R.2
-
49
-
-
0024473893
-
Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol
-
Nelson JW, Kallenbach NR. 1989. Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol. Biochemistry 28:5256-5261.
-
(1989)
Biochemistry
, vol.28
, pp. 5256-5261
-
-
Nelson, J.W.1
Kallenbach, N.R.2
-
50
-
-
0021114569
-
"Molten-globule state": A compact form of globular proteins with mobile side chains
-
Ohgushi M, Wada A. 1983. "Molten-globule state": A compact form of globular proteins with mobile side chains. FEBS Letters 164:21-24.
-
(1983)
FEBS Letters
, vol.164
, pp. 21-24
-
-
Ohgushi, M.1
Wada, A.2
-
51
-
-
0017225714
-
Thermodynamic investigation of proteins III. Thermodynamics description of lysozyme
-
Pfeil W, Privalov PL. 1976. Thermodynamic investigation of proteins III. Thermodynamics description of lysozyme. Biophys Chem 4:41-50.
-
(1976)
Biophys Chem
, vol.4
, pp. 41-50
-
-
Pfeil, W.1
Privalov, P.L.2
-
52
-
-
0018588511
-
Stability of proteins, small globular proteins
-
Privalov PL. 1979. Stability of proteins, small globular proteins. Adv Protein Chem 33:167-241.
-
(1979)
Adv Protein Chem
, vol.33
, pp. 167-241
-
-
Privalov, P.L.1
-
53
-
-
0002940127
-
The molten globule state
-
Creighton TE, ed. New York: W. H. Freeman and Company
-
Ptitsyn OB. 1992. The molten globule state. In: Creighton TE, ed. Protein folding. New York: W. H. Freeman and Company. pp 243-300.
-
(1992)
Protein Folding
, pp. 243-300
-
-
Ptitsyn, O.B.1
-
54
-
-
0028917296
-
Structures of folding intermediates
-
Ptitsyn OB. 1995. Structures of folding intermediates. Curr Opin Struct Biol 5:74-78.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 74-78
-
-
Ptitsyn, O.B.1
-
55
-
-
0024284779
-
Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution
-
Redfield C, Dobson CM. 1988. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry 27:122-136.
-
(1988)
Biochemistry
, vol.27
, pp. 122-136
-
-
Redfield, C.1
Dobson, C.M.2
-
56
-
-
0026751786
-
The folding of the lysozyme involves partially structured intermediates and multiple pathway
-
Radford SE, Dobson CM, Evans PA. 1992. The folding of the lysozyme involves partially structured intermediates and multiple pathway. Nature 358:302-307.
-
(1992)
Nature
, vol.358
, pp. 302-307
-
-
Radford, S.E.1
Dobson, C.M.2
Evans, P.A.3
-
57
-
-
0026143167
-
Local structure in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix-forming or -breaking propensity of peptide segments
-
Segawa S, Fukuno T, Fujiwara K, Noda Y. 1991. Local structure in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix-forming or -breaking propensity of peptide segments. Biopolymers 31:497-509.
-
(1991)
Biopolymers
, vol.31
, pp. 497-509
-
-
Segawa, S.1
Fukuno, T.2
Fujiwara, K.3
Noda, Y.4
-
58
-
-
0026096545
-
Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
-
Semisotnov GV, Rodionova NA, Razgulyaev OT, Uversky VN, Gripas AF, Gilmanshin RI. 1991. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31:119-128.
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.T.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
59
-
-
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 245:180-194.
-
(1995)
J Mol Biol
, vol.245
, pp. 180-194
-
-
Shiraki, K.1
Nishikawa, K.2
Goto, Y.3
-
61
-
-
0014718113
-
Protein denaturation. C. Theoretical models for the mechanism of denaturation
-
Tanford C. 1970. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Advan Protein Chem 24:1-95.
-
(1970)
Advan Protein Chem
, vol.24
, pp. 1-95
-
-
Tanford, C.1
-
62
-
-
0027484016
-
Local and non-local interactions in globular proteins and mechanism of alcohol denaturation
-
Thomas PD, Dill KA. 1993. Local and non-local interactions in globular proteins and mechanism of alcohol denaturation. Protein Sci 2:2050-2065.
-
(1993)
Protein Sci
, vol.2
, pp. 2050-2065
-
-
Thomas, P.D.1
Dill, K.A.2
-
63
-
-
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, Hiragi Y, Kataoka M, Inoko Y, Amemiya Y, Izumi Y, Tagawa H, Muraga 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
Hiragi, Y.2
Kataoka, M.3
Inoko, Y.4
Amemiya, Y.5
Izumi, Y.6
Tagawa, H.7
Muraga, Y.8
-
64
-
-
0026597879
-
The chemical shift index. A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
-
Wishart DS, Stokes BD, Richards FM. 1992. The chemical shift index. A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.
-
(1992)
Biochemistry
, vol.31
, pp. 1647-1651
-
-
Wishart, D.S.1
Stokes, B.D.2
Richards, F.M.3
|