-
1
-
-
0017367552
-
Evidence from rotatory measurements for an intermediate state in the guanidine hydrochloride denaturation of β-lactoglobulin
-
Ananthanarayanan V. S., Ahmad F. Evidence from rotatory measurements for an intermediate state in the guanidine hydrochloride denaturation of β-lactoglobulin. Can. J. Biochem. 55:1977;239-243.
-
(1977)
Can. J. Biochem.
, vol.55
, pp. 239-243
-
-
Ananthanarayanan, V.S.1
Ahmad, F.2
-
3
-
-
0029249945
-
The nature of protein folding pathways: The classic versus the new view
-
Baldwin R. L. The nature of protein folding pathways: the classic versus the new view. J. Biomol. NMR. 5:1995;103-109.
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 103-109
-
-
Baldwin, R.L.1
-
4
-
-
0028947257
-
Funnels, pathways, and the energy landscape of protein folding: A synthesis
-
Bryngelson J. P., Onuchic J. N., Socci N. D., Wolynes P. G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins: Struct. Funct. Genet. 21:1995;167-195.
-
(1995)
Proteins: Struct. Funct. Genet.
, vol.21
, pp. 167-195
-
-
Bryngelson, J.P.1
Onuchic, J.N.2
Socci, N.D.3
Wolynes, P.G.4
-
5
-
-
1842298212
-
From Levinthal to pathways to funnels
-
Dill K. A., Chan H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 10-19
-
-
Dill, K.A.1
Chan, H.S.2
-
6
-
-
0028053187
-
Understanding how proteins fold: The lysozyme story so far
-
Dobson C. M., Evans P. A., Radford S. E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19:1994;31-37.
-
(1994)
Trends Biochem. Sci.
, vol.19
, pp. 31-37
-
-
Dobson, C.M.1
Evans, P.A.2
Radford, S.E.3
-
7
-
-
0030587856
-
Fast events in protein folding
-
Eaton W. A., Thompson P. A., Chan C.-K., Hagen S. J., Hofrichter J. Fast events in protein folding. Structure. 4:1996;1133-1139.
-
(1996)
Structure
, vol.4
, pp. 1133-1139
-
-
Eaton, W.A.1
Thompson, P.A.2
Chan, C.-K.3
Hagen, S.J.4
Hofrichter, J.5
-
8
-
-
0028856785
-
Optimization of rates of protein folding: The nucleation-condensation mechanism and its implication
-
Fersht A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implication. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873.
-
(1995)
Proc. Natl Acad. Sci. USA
, vol.92
, pp. 10869-10873
-
-
Fersht, A.R.1
-
9
-
-
0019331472
-
Spectroscopic characterization of β-lactoglobulin-retinol complex
-
Fugate R. G., Song P.-S. Spectroscopic characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta. 625:1980;28-42.
-
(1980)
Biochim. Biophys. Acta
, vol.625
, pp. 28-42
-
-
Fugate, R.G.1
Song, P.-S.2
-
10
-
-
0028944346
-
Is burst hydrophobic collapse necessary for protein folding?
-
Gutin A. M., Abkevich V. I., Shakhnovich E. I. Is burst hydrophobic collapse necessary for protein folding? Biochemistry. 34:1995;3066-3076.
-
(1995)
Biochemistry
, vol.34
, pp. 3066-3076
-
-
Gutin, A.M.1
Abkevich, V.I.2
Shakhnovich, E.I.3
-
11
-
-
0028346251
-
Comparison of the conformational stability of the molten globule and native states of horse cytochromec
-
Hagihara Y., Tan Y., Goto Y. Comparison of the conformational stability of the molten globule and native states of horse cytochromec. J. Mol. Biol. 237:1994;336-348.
-
(1994)
J. Mol. Biol.
, vol.237
, pp. 336-348
-
-
Hagihara, Y.1
Tan, Y.2
Goto, Y.3
-
12
-
-
0029588554
-
High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
-
Hamada D., Kuroda Y., Tanaka T., Goto Y. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254:1995;737-740.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 737-740
-
-
Hamada, D.1
Kuroda, Y.2
Tanaka, T.3
Goto, Y.4
-
13
-
-
0029740071
-
Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
-
Hamada D., Segawa S., Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol. 3:1996;868-873.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 868-873
-
-
Hamada, D.1
Segawa, S.2
Goto, Y.3
-
14
-
-
0027177971
-
Metal ion-dependent modulation of the dynamics of a designed protein
-
Handel T. M., Williams S. A., DeGrado W. F. Metal ion-dependent modulation of the dynamics of a designed protein. Science. 261:1993;879-885.
-
(1993)
Science
, vol.261
, pp. 879-885
-
-
Handel, T.M.1
Williams, S.A.2
DeGrado, W.F.3
-
15
-
-
0028868995
-
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
-
Itzhaki L. S., Otzen D. E., Fersht A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254:1995;260-288.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 260-288
-
-
Itzhaki, L.S.1
Otzen, D.E.2
Fersht, A.R.3
-
16
-
-
0029893286
-
The methanol-induced globular and expanded denatured states of cytochromec
-
Kamatari Y. O., Konno T., Kataoka M., Akasaka K. The methanol-induced globular and expanded denatured states of cytochromec. J. Mol. Biol. 259:1996;512-523.
-
(1996)
J. Mol. Biol.
, vol.259
, pp. 512-523
-
-
Kamatari, Y.O.1
Konno, T.2
Kataoka, M.3
Akasaka, K.4
-
17
-
-
0025345415
-
Intermediates in the folding reactions of small proteins
-
Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
-
(1990)
Annu. Rev. Biochem.
, vol.59
, pp. 631-660
-
-
Kim, P.S.1
Baldwin, R.L.2
-
18
-
-
0029003514
-
Folding of a four-helix bundle: Studies of acyl-coenzyme A binding protein
-
Kragelund B. B., Robinson C. V., Knudsen J., Dobson C. M., Poulsen F. M. Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry. 34:1995;7117-7224.
-
(1995)
Biochemistry
, vol.34
, pp. 7117-7224
-
-
Kragelund, B.B.1
Robinson, C.V.2
Knudsen, J.3
Dobson, C.M.4
Poulsen, F.M.5
-
19
-
-
0030334664
-
High helicity of peptide fragments corresponding to β-sheet regions of β-lactoglobulin observed by 2D-NMR spectroscopy
-
Kuroda Y., Hamada D., Tanaka T., Goto Y. High helicity of peptide fragments corresponding to β-sheet regions of β-lactoglobulin observed by 2D-NMR spectroscopy. Folding Des. 1:1996;243-251.
-
(1996)
Folding Des
, vol.1
, pp. 243-251
-
-
Kuroda, Y.1
Hamada, D.2
Tanaka, T.3
Goto, Y.4
-
20
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103.
-
(1989)
Proteins: Struct. Funct. Genet.
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
21
-
-
0023669402
-
Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
-
Kuwajima K., Yamaya H., Miwa S., Sugai S., Nagamura T. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Letters. 221:1987;115-118.
-
(1987)
FEBS Letters
, vol.221
, pp. 115-118
-
-
Kuwajima, K.1
Yamaya, H.2
Miwa, S.3
Sugai, S.4
Nagamura, T.5
-
22
-
-
0030582679
-
The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
-
Kuwajima K., Yamaya H., Sugai S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264:1996;806-822.
-
(1996)
J. Mol. Biol.
, vol.264
, pp. 806-822
-
-
Kuwajima, K.1
Yamaya, H.2
Sugai, S.3
-
23
-
-
0023661017
-
Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution
-
Monaco H. L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E. E. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197:1987;695-706.
-
(1987)
J. Mol. Biol.
, vol.197
, pp. 695-706
-
-
Monaco, H.L.1
Zanotti, G.2
Spadon, P.3
Bolognesi, M.4
Sawyer, L.5
Eliopoulos, E.E.6
-
24
-
-
0026546881
-
Structural basis of latency in plasminogen activator inhibitor-1
-
Mottenen J., Strand A., Symersky J., Sweet R. M., Danley D. E., Geoghegan K. F., Gerard R. D., Goldsmith E. J. Structural basis of latency in plasminogen activator inhibitor-1. Nature. 355:1992;270-273.
-
(1992)
Nature
, vol.355
, pp. 270-273
-
-
Mottenen, J.1
Strand, A.2
Symersky, J.3
Sweet, R.M.4
Danley, D.E.5
Geoghegan, K.F.6
Gerard, R.D.7
Goldsmith, E.J.8
-
25
-
-
0026326273
-
Predicting protein secondary structure based on amino acid sequence
-
Nishikawa K., Noguchi T. Predicting protein secondary structure based on amino acid sequence. Methods Enzymol. 202:1991;31-44.
-
(1991)
Methods Enzymol.
, vol.202
, pp. 31-44
-
-
Nishikawa, K.1
Noguchi, T.2
-
26
-
-
0021114569
-
Molten globule state: A compact form of globular proteins with mobile side-chains
-
Ohgushi M., Wada A. Molten globule state: a compact form of globular proteins with mobile side-chains. FEBS Letters. 164:1983;21-24.
-
(1983)
FEBS Letters
, vol.164
, pp. 21-24
-
-
Ohgushi, M.1
Wada, A.2
-
27
-
-
0022931198
-
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
-
Papiz M. Z., Sawyer L., Eliopoulos E. E., North A. C. T., Findlay J. B. C., Sivaprasadarao R., Jones T. A., Newcomer M. E., Kraulis P. J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature. 324:1986;383-385.
-
(1986)
Nature
, vol.324
, pp. 383-385
-
-
Papiz, M.Z.1
Sawyer, L.2
Eliopoulos, E.E.3
North, A.C.T.4
Findlay, J.B.C.5
Sivaprasadarao, R.6
Jones, T.A.7
Newcomer, M.E.8
Kraulis, P.J.9
-
28
-
-
0021876620
-
Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC
-
Pervaiz S., Brew K. Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC. Science. 228:1985;335-337.
-
(1985)
Science
, vol.228
, pp. 335-337
-
-
Pervaiz, S.1
Brew, K.2
-
29
-
-
0002940127
-
The molten globule state
-
New York: W. H. Freeman and Company
-
Ptitsyn O. B. The molten globule state. Protein Folding. 1992;W. H. Freeman and Company, New York.
-
(1992)
Protein Folding
-
-
Ptitsyn, O.B.1
-
30
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn O. B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-229.
-
(1995)
Advan. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
31
-
-
0029904097
-
Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme
-
Rothwarf D. M., Scheraga H. A. Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry. 35:1996;13797-13807.
-
(1996)
Biochemistry
, vol.35
, pp. 13797-13807
-
-
Rothwarf, D.M.1
Scheraga, H.A.2
-
33
-
-
0028978422
-
Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
-
Shiraki K., Nishikawa K., Goto Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245:1995;180-194.
-
(1995)
J. Mol. Biol.
, vol.245
, pp. 180-194
-
-
Shiraki, K.1
Nishikawa, K.2
Goto, Y.3
-
34
-
-
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. The concept of a random coil residual structure in peptides and denatured proteins. Folding Des. 1:1996;R95-R106.
-
(1996)
Folding Des
, vol.1
-
-
Smith, L.J.1
Fiebig, K.M.2
Schwalbe, H.3
Dobson, C.M.4
-
35
-
-
0024293204
-
Conformation of peptide fragments of proteins in aqueous solution: Implication for initiation of protein folding
-
Wright P. E., Dyson H. J., Lenner R. A. Conformation of peptide fragments of proteins in aqueous solution: implication for initiation of protein folding. Biochemistry. 27:1988;7164-7175.
-
(1988)
Biochemistry
, vol.27
, pp. 7164-7175
-
-
Wright, P.E.1
Dyson, H.J.2
Lenner, R.A.3
-
36
-
-
0022503457
-
Calculation of protein conformation from circular dichroism
-
Yang J. T., Wu C. S., Martinez H. M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1986;208-269.
-
(1986)
Methods Enzymol.
, vol.130
, pp. 208-269
-
-
Yang, J.T.1
Wu, C.S.2
Martinez, H.M.3
|