-
1
-
-
0027008444
-
1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea-pig α-lactalbumin
-
1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea-pig α-lactalbumin. Eur J Biochem 210:699-709.
-
(1992)
Eur J Biochem
, vol.210
, pp. 699-709
-
-
Alexandrescu, A.T.1
Broadhurst, R.W.2
Wormald, C.3
Chyan, C.L.4
Baum, J.5
Bychkova, V.E.6
Lebedev, Yu.7
Gilmanshin, R.I.8
Semisotnov, G.V.9
Tiktopulo, E.I.10
Dobson, C.M.11
-
2
-
-
0027536094
-
Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
-
Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. 1992b. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study. Biochemistry 32:1707-1718.
-
(1992)
Biochemistry
, vol.32
, pp. 1707-1718
-
-
Alexandrescu, A.T.1
Evans, P.A.2
Pitkeathly, M.3
Baum, J.4
Dobson, C.M.5
-
3
-
-
0015859467
-
Principles that govern the folding of protein chain
-
Anfinsen CB. 1973. Principles that govern the folding of protein chain. Science 181:223-230.
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
4
-
-
0028776642
-
Matching speed and stability
-
Baldwin RL. 1994. Matching speed and stability. Nature 369:248-251.
-
(1994)
Nature
, vol.369
, pp. 248-251
-
-
Baldwin, R.L.1
-
5
-
-
0027254057
-
The molten globule intermediate of apomyoglobin and the process of protein folding
-
Barrick D, Baldwin RL. 1493. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci 2:869-876.
-
(1493)
Protein Sci
, vol.2
, pp. 869-876
-
-
Barrick, D.1
Baldwin, R.L.2
-
6
-
-
0024533979
-
Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea-pig α-lactalbumin
-
Baum J, Dobson CM, Evans PA, Hanley C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea-pig α-lactalbumin. Biochemistry 28:7-13.
-
(1989)
Biochemistry
, vol.28
, pp. 7-13
-
-
Baum, J.1
Dobson, C.M.2
Evans, P.A.3
Hanley, C.4
-
7
-
-
0014952474
-
Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease a
-
Brandts JF, Oliveria RJ, Westort C. 1970. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9:1038-1047.
-
(1970)
Biochemistry
, vol.9
, pp. 1038-1047
-
-
Brandts, J.F.1
Oliveria, R.J.2
Westort, C.3
-
8
-
-
0031790423
-
Thermodynamic analysis of biomolecules: A volumetric approach
-
Chalikian TV, Breslauer KJ. 1998. Thermodynamic analysis of biomolecules: A volumetric approach. Curr Opin Struct Biol 8:657-664.
-
(1998)
Curr Opin Struct Biol
, vol.8
, pp. 657-664
-
-
Chalikian, T.V.1
Breslauer, K.J.2
-
9
-
-
0029011017
-
Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
-
Chalikian TV, Gindikin VS, Breslauer KJ. 1995. Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH. J Mol Biol 250:291-306
-
(1995)
J Mol Biol
, vol.250
, pp. 291-306
-
-
Chalikian, T.V.1
Gindikin, V.S.2
Breslauer, K.J.3
-
10
-
-
0343247668
-
The native and the heat-induced denatured states of α-chymotrypsinogen a: Thermodynamic and spectroscopic studies
-
Chalikian TV, Völker J, Anafi D, Breslauer KJ. 1997. The native and the heat-Induced denatured states of α-chymotrypsinogen A: Thermodynamic and spectroscopic studies. J Mol Biol 274:237-252.
-
(1997)
J Mol Biol
, vol.274
, pp. 237-252
-
-
Chalikian, T.V.1
Völker, J.2
Anafi, D.3
Breslauer, K.J.4
-
11
-
-
0033593529
-
Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli
-
Chaudhuri TK, Horii K, Yoda T, Arai M, Nagata S, Terada TP, Uchiyama H, Ikura T, Tsumoto, K, Kataoka H, et al. 1999. Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli. J Mol Biol 285:1179-1194.
-
(1999)
J Mol Biol
, vol.285
, pp. 1179-1194
-
-
Chaudhuri, T.K.1
Horii, K.2
Yoda, T.3
Arai, M.4
Nagata, S.5
Terada, T.P.6
Uchiyama, H.7
Ikura, T.8
Tsumoto, K.9
Kataoka, H.10
-
12
-
-
0027280472
-
Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study
-
Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J. 1993. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study. Biochemistry 32:5681-5691.
-
(1993)
Biochemistry
, vol.32
, pp. 5681-5691
-
-
Chyan, C.L.1
Wormald, C.2
Dobson, C.M.3
Evans, P.A.4
Baum, J.5
-
17
-
-
0022370492
-
Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin
-
Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bushuev VN, Bychkova VE, Lebedev Yu, Gilmanshin RI, Semisotnov GV, Tiktopulo EI, Ptitsyn OB. 1985. Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin. Eur Biophys J 13:109-121.
-
(1985)
Eur Biophys J
, vol.13
, pp. 109-121
-
-
Dolgikh, D.A.1
Abaturov, L.V.2
Bolotina, I.A.3
Brazhnikov, E.V.4
Bushuev, V.N.5
Bychkova, V.E.6
Lebedev, Yu.7
Gilmanshin, R.I.8
Semisotnov, G.V.9
Tiktopulo, E.I.10
Ptitsyn, O.B.11
-
18
-
-
0029070645
-
Volume changes of the molten globule transitions of horse heart ferricytochrome c: A thermodynamic cycle
-
Foygel K, Spector S, Chatterjee S, Kahn PC. 1995. Volume changes of the molten globule transitions of horse heart ferricytochrome c: A thermodynamic cycle. Protein Sci 4:1426-1429.
-
(1995)
Protein Sci
, vol.4
, pp. 1426-1429
-
-
Foygel, K.1
Spector, S.2
Chatterjee, S.3
Kahn, P.C.4
-
19
-
-
0029737544
-
Testing the correlation between ΔA and ΔV of protein unfolding using m value mutants of staphylococcal nuclease
-
Frye KJ, Perman CS, Royer CA. 1996. Testing the correlation between ΔA and ΔV of protein unfolding using m value mutants of staphylococcal nuclease. Biochemistry 35:10234-10239.
-
(1996)
Biochemistry
, vol.35
, pp. 10234-10239
-
-
Frye, K.J.1
Perman, C.S.2
Royer, C.A.3
-
20
-
-
0025774449
-
Anion and ph-dependent conformational transition of an amphiphilic polypeptide
-
Goto Y, Aimoto S. 1991. Anion and pH-dependent conformational transition of an amphiphilic polypeptide. J Mol Biol 218:387-396.
-
(1991)
J Mol Biol
, vol.218
, pp. 387-396
-
-
Goto, Y.1
Aimoto, S.2
-
21
-
-
0028174361
-
Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
-
Griko YV, Freire E, Privalov PL. 1994. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
-
(1994)
Biochemistry
, vol.33
, pp. 1889-1899
-
-
Griko, Y.V.1
Freire, E.2
Privalov, P.L.3
-
22
-
-
0028329347
-
Thermodynamic puzzle of apomyoglobin unfolding
-
Griko YV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
-
(1994)
J Mol Biol
, vol.235
, pp. 1318-1325
-
-
Griko, Y.V.1
Privalov, P.L.2
-
23
-
-
0015236387
-
Reversible pressure and temperature denaturation of chymotrypsinogen
-
Hawley SA. 1971. Reversible pressure and temperature denaturation of chymotrypsinogen. Biochemistry 10:2436-2442.
-
(1971)
Biochemistry
, vol.10
, pp. 2436-2442
-
-
Hawley, S.A.1
-
24
-
-
0022122037
-
Equilibrium and kinetic study of sodium- and potassium-induced conformational change of apo-α-lactalbumin
-
Hiraoka Y, Sugai S. 1985. Equilibrium and kinetic study of sodium- and potassium-induced conformational change of apo-α-lactalbumin. Int J Peptide Protein Res 26:252-261.
-
(1985)
Int J Peptide Protein Res
, vol.26
, pp. 252-261
-
-
Hiraoka, Y.1
Sugai, S.2
-
25
-
-
0022702283
-
2+-induced alteration in the unfolding behavior of α-lactalbumin
-
2+-Induced alteration in the unfolding behavior of α-lactalbumin. J Biochem 99:1191-1201.
-
(1986)
J Biochem
, vol.99
, pp. 1191-1201
-
-
Ikeguchi, M.1
Kuwajima, K.2
Sugai, S.3
-
27
-
-
0008863560
-
Some factors in the interpretation of protein denaturation
-
Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
-
(1959)
Adv Protein Chem
, vol.14
, pp. 1-63
-
-
Kauzmann, W.1
-
28
-
-
0031019791
-
Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior
-
Kharakoz DP, Bychkova VE. 1997. Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior. Biochemistry 36: 1882-1890.
-
(1997)
Biochemistry
, vol.36
, pp. 1882-1890
-
-
Kharakoz, D.P.1
Bychkova, V.E.2
-
29
-
-
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
-
32
-
-
0017399699
-
A folding model of α-lactalbumin deduced from the three-state denaturation mechanism
-
Kuwajima K. 1977. A folding model of α-lactalbumin deduced from the three-state denaturation mechanism. J Mol Biol 114:241-258.
-
(1977)
J Mol Biol
, vol.114
, pp. 241-258
-
-
Kuwajima, K.1
-
33
-
-
0022559769
-
2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra
-
2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra. Int J Peptide Protein Res 27:18-27.
-
(1986)
Int J Peptide Protein Res
, vol.27
, pp. 18-27
-
-
Kuwajima, K.1
Harushima, Y.2
Sugai, S.3
-
34
-
-
0017178548
-
Three-state denaturation of α-lactalbumin by guanidine hydrochloride
-
Kuwajima K, Nitta K, Yoneyama M, Sugai S. 1976. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J Mol Biol 106:359-373.
-
(1976)
J Mol Biol
, vol.106
, pp. 359-373
-
-
Kuwajima, K.1
Nitta, K.2
Yoneyama, M.3
Sugai, S.4
-
35
-
-
0014952466
-
Lactose synthetase. Modification of carboxyl groups in α-lactalbumin
-
Lin TY. 1970. Lactose synthetase. Modification of carboxyl groups in α-lactalbumin. Biochemistry 9:984-995.
-
(1970)
Biochemistry
, vol.9
, pp. 984-995
-
-
Lin, T.Y.1
-
36
-
-
0025906146
-
Contribution to the thermodynamics of protein folding from the reduction in water-accessible non-polar surface area
-
Livingstone JR, Spolar RS, Record MT. 1991. Contribution to the thermodynamics of protein folding from the reduction in water-accessible non-polar surface area. Biochemistry 30:4231-4244.
-
(1991)
Biochemistry
, vol.30
, pp. 4231-4244
-
-
Livingstone, J.R.1
Spolar, R.S.2
Record, M.T.3
-
37
-
-
0027305948
-
Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration
-
Makhatadze GI, Privalov PL. 1993. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J Mol Biol 232:639-659.
-
(1993)
J Mol Biol
, vol.232
, pp. 639-659
-
-
Makhatadze, G.I.1
Privalov, P.L.2
-
39
-
-
0014995544
-
Volume and sound velocity changes associated with coil-β transition of poly(S-carboxymethyl L-cysteine) in aqueous solution
-
Makino S, Noguchi H. 1971. Volume and sound velocity changes associated with coil-β transition of poly(S-carboxymethyl L-cysteine) in aqueous solution. Biopolymers 10:1253-1260.
-
(1971)
Biopolymers
, vol.10
, pp. 1253-1260
-
-
Makino, S.1
Noguchi, H.2
-
41
-
-
0025200973
-
The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo
-
Moerschell RP, Hosokawa Y, Tsunasawa S, Sherman F. 1990. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. J Biol Chem 265:19638-19634.
-
(1990)
J Biol Chem
, vol.265
, pp. 19638-119634
-
-
Moerschell, R.P.1
Hosokawa, Y.2
Tsunasawa, S.3
Sherman, F.4
-
42
-
-
0042218504
-
Studies of the helix-coil transition of poly-L-lysine in film and solution
-
Noguchi H. 1966. Studies of the helix-coil transition of poly-L-lysine in film and solution. Biopolymers 4:1105-1113.
-
(1966)
Biopolymers
, vol.4
, pp. 1105-1113
-
-
Noguchi, H.1
-
43
-
-
84984087587
-
Dilatmetric and refractometric studies of the helix-coil transition of poly-L-glutamic acid in aqueous solution
-
Noguchi H, Yang JT. 1963. Dilatmetric and refractometric studies of the helix-coil transition of poly-L-glutamic acid in aqueous solution. Biopolymers 1:359-370.
-
(1963)
Biopolymers
, vol.1
, pp. 359-370
-
-
Noguchi, H.1
Yang, J.T.2
-
44
-
-
0018183085
-
Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin
-
Nozaka M, Kuwajima K, Nitta K, Sugai S. 1978. Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin. Biochemistry 12:3753-3758.
-
(1978)
Biochemistry
, vol.12
, pp. 3753-3758
-
-
Nozaka, M.1
Kuwajima, K.2
Nitta, K.3
Sugai, S.4
-
45
-
-
0015438810
-
The preparation of guanidine hydrochloride
-
Nozaki Y. 1972. The preparation of guanidine hydrochloride. Methods Enzymol 26:43-50.
-
(1972)
Methods Enzymol
, vol.26
, pp. 43-50
-
-
Nozaki, Y.1
-
46
-
-
0028334906
-
A protein dissection study of a molten globule
-
Peng Z-Y, Kim PS. 1994. A protein dissection study of a molten globule. Biochemistry 33:2136-2141.
-
(1994)
Biochemistry
, vol.33
, pp. 2136-2141
-
-
Peng, Z.-Y.1
Kim, P.S.2
-
47
-
-
0030010408
-
Intermediate states in protein folding
-
Privalov PL. 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
-
48
-
-
0024199422
-
Stability of protein structure and hydrophobic interaction
-
Privalov PL, Gill SJ. 1989. Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39:191-234.
-
(1989)
Adv Protein Chem
, vol.39
, pp. 191-234
-
-
Privalov, P.L.1
Gill, S.J.2
-
49
-
-
0343433552
-
Heat capacity of proteins. 2. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
-
Privalov PL, Makhatadze GI. 1990. Heat capacity of proteins. 2. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects. J Mol Biol 213:715-723.
-
(1990)
J Mol Biol
, vol.213
, pp. 715-723
-
-
Privalov, P.L.1
Makhatadze, G.I.2
-
50
-
-
0025212107
-
Evidence for a molten globule state as a general intermediate in protein folding
-
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett 262:20-24.
-
(1990)
FEBS Lett
, vol.262
, pp. 20-24
-
-
Ptitsyn, O.B.1
Pain, R.H.2
Semisotnov, G.V.3
Zerovnik, E.4
Razgulyaev, O.I.5
-
51
-
-
0342997911
-
High-resolution NMR study of the pressure-induced unfolding of lysozyme
-
Samarasinghe SD, Campbell DM, Jonas A, Jonas J. 1992. High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry 32:5222-5232.
-
(1992)
Biochemistry
, vol.32
, pp. 5222-5232
-
-
Samarasinghe, S.D.1
Campbell, D.M.2
Jonas, A.3
Jonas, J.4
-
52
-
-
0028866620
-
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin
-
Schulman BA, Redfield C, Peng Z-Y, Dobson CM, Kim PS. 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
-
53
-
-
0023657937
-
Sequential mechanism of refolding of carbonic anhydrase B
-
Semisotnov GV, Rodionova NA, Kutyshennko VP, Ebert B, Blank J, Ptitsyn OB. 1987. Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett 224:9-13.
-
(1987)
FEBS Lett
, vol.224
, pp. 9-13
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Kutyshennko, V.P.3
Ebert, B.4
Blank, J.5
Ptitsyn, O.B.6
-
54
-
-
0026096545
-
Study of molten globule intermediate state in protein folding by a hydrophobic fluorescent probe
-
Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas' AF, Gilmanshin RI. 1991. Study of 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.I.3
Uversky, V.N.4
Gripas', A.F.5
Gilmanshin, R.I.6
-
55
-
-
0026684671
-
Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from removal of non-polar and polar surfaces from water
-
Spolar RS, Livingstone JR, Record MT. 1992. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from removal of non-polar and polar surfaces from water. Biochemistry 31:3947-3955.
-
(1992)
Biochemistry
, vol.31
, pp. 3947-3955
-
-
Spolar, R.S.1
Livingstone, J.R.2
Record, M.T.3
-
56
-
-
0015784343
-
Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride
-
Sugai S, Yashiro H, Nitta K. 1973. Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride. Biochim Biophys Acta 328:35-41.
-
(1973)
Biochim Biophys Acta
, vol.328
, pp. 35-41
-
-
Sugai, S.1
Yashiro, H.2
Nitta, K.3
-
57
-
-
0030058251
-
The pressure-induced structural change of bovine α-lactalbumin as studied by a fluorescence hydrophobic probe
-
Tanaka N, Kunugi S. 1996. The pressure-induced structural change of bovine α-lactalbumin as studied by a fluorescence hydrophobic probe. Int J Biol Macromol 18:33-39.
-
(1996)
Int J Biol Macromol
, vol.18
, pp. 33-39
-
-
Tanaka, N.1
Kunugi, S.2
-
58
-
-
0031837399
-
Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
-
Vidugiris GJA, Royer CA. 1998. Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. J Biophys 75:463-470.
-
(1998)
J Biophys
, vol.75
, pp. 463-470
-
-
Vidugiris, G.J.A.1
Royer, C.A.2
-
59
-
-
0015820466
-
Pressure denaturation of metmyoglobin
-
Zipp A, Kauzmann W. 1973. Pressure denaturation of metmyoglobin. Biochemistry 12:4217-4228.
-
(1973)
Biochemistry
, vol.12
, pp. 4217-4228
-
-
Zipp, A.1
Kauzmann, W.2
|