-
1
-
-
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
-
2
-
-
0030059690
-
The molten globule state of α-lactalbumin
-
Kuwajima K. The molten globule state of α-lactalbumin. FASEB J. 10:1996;102-109.
-
(1996)
FASEB J.
, vol.10
, pp. 102-109
-
-
Kuwajima, K.1
-
3
-
-
0034581327
-
Role of the molten globule state in protein folding
-
Arai M., Kuwajima K. Role of the molten globule state in protein folding. Advan. Protein Chem. 53:2000;209-282.
-
(2000)
Advan. Protein Chem.
, vol.53
, pp. 209-282
-
-
Arai, M.1
Kuwajima, K.2
-
4
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548.
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
5
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896.
-
(1993)
Science
, vol.262
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
6
-
-
0022423885
-
Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
-
Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881.
-
(1985)
Biochemistry
, vol.24
, pp. 874-881
-
-
Kuwajima, K.1
Hiraoka, Y.2
Ikeguchi, M.3
Sugai, S.4
-
7
-
-
0023041667
-
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
-
Ikeguchi M., Kuwajima K., Mitani M., Sugai S. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry. 25:1986;6965-6972.
-
(1986)
Biochemistry
, vol.25
, pp. 6965-6972
-
-
Ikeguchi, M.1
Kuwajima, K.2
Mitani, M.3
Sugai, S.4
-
8
-
-
0030348041
-
Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
-
Arai M., Kuwajima K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Des. 1:1996;275-287.
-
(1996)
Fold. Des.
, vol.1
, pp. 275-287
-
-
Arai, M.1
Kuwajima, K.2
-
9
-
-
0033004311
-
Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin
-
Forge V., Wijesinha R.T., Balbach J., Brew K., Robinson C.V., Redfield C., Dobson C.M. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin. J. Mol. Biol. 288:1999;673-688.
-
(1999)
J. Mol. Biol.
, vol.288
, pp. 673-688
-
-
Forge, V.1
Wijesinha, R.T.2
Balbach, J.3
Brew, K.4
Robinson, C.V.5
Redfield, C.6
Dobson, C.M.7
-
10
-
-
0036349865
-
Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering
-
Arai M., Ito K., Inobe T., Nakao M., Maki K., Kamagata K., et al. Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering. J. Mol. Biol. 321:2002;121-132.
-
(2002)
J. Mol. Biol.
, vol.321
, pp. 121-132
-
-
Arai, M.1
Ito, K.2
Inobe, T.3
Nakao, M.4
Maki, K.5
Kamagata, K.6
-
11
-
-
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.-., Dobson C.M., Kim P.S. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J. Mol. Biol. 253:1995;651-657.
-
(1995)
J. Mol. Biol.
, vol.253
, pp. 651-657
-
-
Schulman, B.A.1
Redfield, C.2
Peng, Z.3
Dobson, C.M.4
Kim, P.S.5
-
12
-
-
0030768045
-
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
-
Schulman B.A., Kim P.S., Dobson C.M., Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol. 4:1997;630-634.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 630-634
-
-
Schulman, B.A.1
Kim, P.S.2
Dobson, C.M.3
Redfield, C.4
-
13
-
-
0031932824
-
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
-
Eliezer D., Yao J., Dyson J.H., Wright P.E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol. 5:1998;148-155.
-
(1998)
Nature Struct. Biol.
, vol.5
, pp. 148-155
-
-
Eliezer, D.1
Yao, J.2
Dyson, J.H.3
Wright, P.E.4
-
14
-
-
0342679998
-
Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy
-
Trouiller A., Reinstadler D., Dupont Y., Naumann D., Forge V. Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy. Nature Struct. Biol. 7:2000;78-86.
-
(2000)
Nature Struct. Biol.
, vol.7
, pp. 78-86
-
-
Trouiller, A.1
Reinstadler, D.2
Dupont, Y.3
Naumann, D.4
Forge, V.5
-
15
-
-
0024533979
-
Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
-
Baum J., Dobson C.M., Evans P.A., Hanley C. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry. 28:1989;7-13.
-
(1989)
Biochemistry
, vol.28
, pp. 7-13
-
-
Baum, J.1
Dobson, C.M.2
Evans, P.A.3
Hanley, C.4
-
16
-
-
0025916703
-
Crystal structure of human α-lactalbumin at 1.7 Å resolution
-
Acharya K.R., Ren J.S., Stuart D.I., Phillips D.C., Fenna R.E. Crystal structure of human α-lactalbumin at 1.7 Å resolution. J. Mol. Biol. 221:1991;571-581.
-
(1991)
J. Mol. Biol.
, vol.221
, pp. 571-581
-
-
Acharya, K.R.1
Ren, J.S.2
Stuart, D.I.3
Phillips, D.C.4
Fenna, R.E.5
-
17
-
-
0022370492
-
Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin
-
Dolgikh D.A., Abaturov L.V., Bolotina I.A., Brazhnikov E.V., Bychkova V.E., Bushuev V.N., et al. Compact state of a protein molecule with pronounced small-scale mobility: bovine α-lactalbumin. Eur. Biophys. J. 13:1985;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
Bychkova, V.E.5
Bushuev, V.N.6
-
18
-
-
0032825667
-
α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds
-
Redfield C., Schulman B.A., Milhollen M.A., Kim P.S., Dobson C.M. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds. Nature Struct. Biol. 6:1999;948-952.
-
(1999)
Nature Struct. Biol.
, vol.6
, pp. 948-952
-
-
Redfield, C.1
Schulman, B.A.2
Milhollen, M.A.3
Kim, P.S.4
Dobson, C.M.5
-
19
-
-
0019890466
-
α-Lactalbumin: Compact state with fluctuating tertiary structure?
-
Dolgikh D.A., Gilmanshin R.I., Brazhnikov E.V., Bychkova V.E., Semisotnov G.V., Venyaminov S.Y., Ptitsyn O.B. α-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Letters. 136:1981;311-315.
-
(1981)
FEBS Letters
, vol.136
, pp. 311-315
-
-
Dolgikh, D.A.1
Gilmanshin, R.I.2
Brazhnikov, E.V.3
Bychkova, V.E.4
Semisotnov, G.V.5
Venyaminov, S.Y.6
Ptitsyn, O.B.7
-
20
-
-
0028952169
-
Bipartite structure of the α-lactalbumin molten globule
-
Wu L.C., Peng Z.-., Kim P.S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2:1995;281-286.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 281-286
-
-
Wu, L.C.1
Peng, Z.2
Kim, P.S.3
-
21
-
-
0032479440
-
A specific hydrophobic core in the α-lactalbumin molten globule
-
Wu L.C., Kim P.S. A specific hydrophobic core in the α-lactalbumin molten globule. J. Mol. Biol. 280:1998;175-182.
-
(1998)
J. Mol. Biol.
, vol.280
, pp. 175-182
-
-
Wu, L.C.1
Kim, P.S.2
-
22
-
-
0028814936
-
Probing the molten globule state of α-lactalbumin by limited proteolysis
-
Polverino de Laureto P., DeFilippis V., DiBello M., Zambonin M., Fontana A. Probing the molten globule state of α-lactalbumin by limited proteolysis. Biochemistry. 34:1995;12596-12604.
-
(1995)
Biochemistry
, vol.34
, pp. 12596-12604
-
-
Polverino de Laureto, P.1
DeFilippis, V.2
DiBello, M.3
Zambonin, M.4
Fontana, A.5
-
23
-
-
0029123975
-
Following protein folding in real time using NMR spectroscopy
-
Balbach J., Forge V., Lau W.S., Van Nuland N.A., Winder S.L., Hore P.J., Dobson C.M. Following protein folding in real time using NMR spectroscopy. Nature Struct. Biol. 2:1995;865-870.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 865-870
-
-
Balbach, J.1
Forge, V.2
Lau, W.S.3
Van Nuland, N.A.4
Winder, S.L.5
Hore, P.J.6
Dobson, C.M.7
-
24
-
-
0034687724
-
Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy
-
Chaudhuri T.K., Arai M., Terada T.P., Ikura T., Kuwajima K. Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy. Biochemistry. 39:2000;15643-15651.
-
(2000)
Biochemistry
, vol.39
, pp. 15643-15651
-
-
Chaudhuri, T.K.1
Arai, M.2
Terada, T.P.3
Ikura, T.4
Kuwajima, K.5
-
25
-
-
0032698757
-
Limited proteolysis of bovine α-lactalbumin: Isolation and characterization of protein domains
-
Polverino de Laureto P., Scaramella E., Frigo M., Wondrich F.G., DeFilippis V., Zambonin M., Fontana A. Limited proteolysis of bovine α-lactalbumin: isolation and characterization of protein domains. Protein Sci. 8:1999;2290-2303.
-
(1999)
Protein Sci.
, vol.8
, pp. 2290-2303
-
-
Polverino de Laureto, P.1
Scaramella, E.2
Frigo, M.3
Wondrich, F.G.4
DeFilippis, V.5
Zambonin, M.6
Fontana, A.7
-
26
-
-
0035807845
-
Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway
-
Cavagnero S., Nishimura C., Schwarzinger S., Dyson H.J., Wright P.E. Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway. Biochemistry. 40:2001;14459-14467.
-
(2001)
Biochemistry
, vol.40
, pp. 14459-14467
-
-
Cavagnero, S.1
Nishimura, C.2
Schwarzinger, S.3
Dyson, H.J.4
Wright, P.E.5
-
27
-
-
0035823118
-
Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules
-
Wijesinha-Bettoni R., Dobson C.M., Redfield C. Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules. J. Mol. Biol. 312:2001;261-273.
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 261-273
-
-
Wijesinha-Bettoni, R.1
Dobson, C.M.2
Redfield, C.3
-
28
-
-
0028856228
-
The equilibrium folding pathway of staphylococcal nuclease: Indefitication of the most stable chain-chain interactions by NMR and CD spectroscopy
-
Wang Y., Shortle D. The equilibrium folding pathway of staphylococcal nuclease: indefitication of the most stable chain-chain interactions by NMR and CD spectroscopy. Biochemistry. 34:1995;15895-15905.
-
(1995)
Biochemistry
, vol.34
, pp. 15895-15905
-
-
Wang, Y.1
Shortle, D.2
-
29
-
-
0029786948
-
A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
-
Wang Y., Shortle D. A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease. Protein Sci. 5:1996;1898-1906.
-
(1996)
Protein Sci.
, vol.5
, pp. 1898-1906
-
-
Wang, Y.1
Shortle, D.2
-
30
-
-
0031064317
-
Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
-
Zhang O., Forman-Kay J.D., Shortle D., Kay L.E. Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins. J. Biomol. NMR. 9:1997;181-200.
-
(1997)
J. Biomol. NMR
, vol.9
, pp. 181-200
-
-
Zhang, O.1
Forman-Kay, J.D.2
Shortle, D.3
Kay, L.E.4
-
31
-
-
0032539590
-
Molten globule unfolding monitored by hydrogen exchange in urea
-
Chamberlain A.K., Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry. 37:1998;1736-1742.
-
(1998)
Biochemistry
, vol.37
, pp. 1736-1742
-
-
Chamberlain, A.K.1
Marqusee, S.2
-
32
-
-
0026679847
-
Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry
-
Yutani K., Ogasahara K., Kuwajima K. Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry. J. Mol. Biol. 228:1992;347-350.
-
(1992)
J. Mol. Biol.
, vol.228
, pp. 347-350
-
-
Yutani, K.1
Ogasahara, K.2
Kuwajima, K.3
-
33
-
-
0026096545
-
Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe
-
Semisotnov G.V., Rodionova N.A., Razgulyaev O.J., Uversky V.N., Gripas A.F., Gilmanshin R.I. Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31:1991;119-128.
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.J.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
35
-
-
0033607727
-
Characterization of millisecond time-scale dynamics in the molten globule state of α-lactalbumin by NMR
-
Kim S., Bracken C., Baum J. Characterization of millisecond time-scale dynamics in the molten globule state of α-lactalbumin by NMR. J. Mol. Biol. 294:1999;551-560.
-
(1999)
J. Mol. Biol.
, vol.294
, pp. 551-560
-
-
Kim, S.1
Bracken, C.2
Baum, J.3
-
36
-
-
0030726758
-
Populating the equilibrium molten globule state of apomyoglobin under suitable conditions for structural characterization by NMR
-
Eliezar D., Jennings P.A., Dyson H.J., Wright P.E. Populating the equilibrium molten globule state of apomyoglobin under suitable conditions for structural characterization by NMR. FEBS Letters. 417:1997;92-96.
-
(1997)
FEBS Letters
, vol.417
, pp. 92-96
-
-
Eliezar, D.1
Jennings, P.A.2
Dyson, H.J.3
Wright, P.E.4
-
37
-
-
0028061408
-
Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
-
Gast K., Damaschun H., Misselwitz R., Mller-Frohne M., Zirwer D., Damaschun G. Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate. Eur. Biophys. J. 23:1994;297-305.
-
(1994)
Eur. Biophys. J.
, vol.23
, pp. 297-305
-
-
Gast, K.1
Damaschun, H.2
Misselwitz, R.3
Mller-Frohne, M.4
Zirwer, D.5
Damaschun, G.6
-
39
-
-
0035943398
-
Probing subtle differences in the hydrogen exchange behavior of variants of the human α-lactalbumin molten globule using mass spectrometry
-
Last A.M., Schulman B.A., Robinson C.V., Redfield C. Probing subtle differences in the hydrogen exchange behavior of variants of the human α-lactalbumin molten globule using mass spectrometry. J. Mol. Biol. 311:2001;909-919.
-
(2001)
J. Mol. Biol.
, vol.311
, pp. 909-919
-
-
Last, A.M.1
Schulman, B.A.2
Robinson, C.V.3
Redfield, C.4
-
40
-
-
0032538350
-
Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin
-
Demarest S.J., Fairman R., Raleigh D.P. Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin. J. Mol. Biol. 283:1998;279-291.
-
(1998)
J. Mol. Biol.
, vol.283
, pp. 279-291
-
-
Demarest, S.J.1
Fairman, R.2
Raleigh, D.P.3
-
41
-
-
0030993346
-
Calcium binding peptides from α-lactalbumin: Implications for protein folding and stability
-
Kuhlman B., Boice J.A., Wu W.-J., Fairman R., Raleigh D.P. Calcium binding peptides from α-lactalbumin: implications for protein folding and stability. Biochemistry. 36:1997;4607-4615.
-
(1997)
Biochemistry
, vol.36
, pp. 4607-4615
-
-
Kuhlman, B.1
Boice, J.A.2
Wu, W.-J.3
Fairman, R.4
Raleigh, D.P.5
-
42
-
-
0029894160
-
A synthetic peptide study on the molten globule of α-lactalbumin
-
Shimizu A., Ikeguchi M., Kobayashi T., Sugai S. A synthetic peptide study on the molten globule of α-lactalbumin. J. Biochem. 119:1996;947-952.
-
(1996)
J. Biochem.
, vol.119
, pp. 947-952
-
-
Shimizu, A.1
Ikeguchi, M.2
Kobayashi, T.3
Sugai, S.4
-
43
-
-
0034141812
-
Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of non-native structure in the denatured state
-
Demarest S.J., Raleigh D.P. Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of non-native structure in the denatured state. Proteins: Struct. Funct. Genet. 38:2000;189-196.
-
(2000)
Proteins: Struct. Funct. Genet.
, vol.38
, pp. 189-196
-
-
Demarest, S.J.1
Raleigh, D.P.2
-
44
-
-
0035254984
-
A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin
-
Demarest S.J., Horng J.-C., Raleigh D.P. A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin. Proteins: Struct. Funct. Genet. 42:2001;237-242.
-
(2001)
Proteins: Struct. Funct. Genet.
, vol.42
, pp. 237-242
-
-
Demarest, S.J.1
Horng, J.-C.2
Raleigh, D.P.3
-
45
-
-
0033584978
-
Defining the core structure of the α-lactalbumin molten globule state
-
Demarest S.J., Boice J.A., Fairman R., Raleigh D.P. Defining the core structure of the α-lactalbumin molten globule state. J. Mol. Biol. 294:1999;213-221.
-
(1999)
J. Mol. Biol.
, vol.294
, pp. 213-221
-
-
Demarest, S.J.1
Boice, J.A.2
Fairman, R.3
Raleigh, D.P.4
-
46
-
-
0034685617
-
Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin
-
Mizuguchi M., Masaki K., Demura M., Nitta K. Local and long-range interactions in the molten globule state: a study of chimeric proteins of bovine and human α-lactalbumin. J. Mol. Biol. 298:2000;985-995.
-
(2000)
J. Mol. Biol.
, vol.298
, pp. 985-995
-
-
Mizuguchi, M.1
Masaki, K.2
Demura, M.3
Nitta, K.4
-
47
-
-
0028009873
-
Characterization of a trifluoroethanol-induced partially folded states of α-lactalbumin
-
Alexandrescu A.T., Ng Y.L., Dobson C.M. Characterization of a trifluoroethanol-induced partially folded states of α-lactalbumin. J. Mol. Biol. 235:1994;587-599.
-
(1994)
J. Mol. Biol.
, vol.235
, pp. 587-599
-
-
Alexandrescu, A.T.1
Ng, Y.L.2
Dobson, C.M.3
-
48
-
-
0028882136
-
Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol
-
Buck M., Schwalbe H., Dobson C.M. Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry. 34:1995;13219-13232.
-
(1995)
Biochemistry
, vol.34
, pp. 13219-13232
-
-
Buck, M.1
Schwalbe, H.2
Dobson, C.M.3
-
49
-
-
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. 257:1996;669-683.
-
(1996)
J. Mol. Biol.
, vol.257
, pp. 669-683
-
-
Buck, M.1
Schwalbe, H.2
Dobson, C.M.3
-
50
-
-
0033593529
-
Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli
-
Chaudhuri T.K., Horii K., Yoda T., Arai M., Nagata S., Terada T.P., et al. Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli. J. Mol. Biol. 285:1999;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
-
51
-
-
0026793589
-
Kinetic resolution of peptide bond and side chain far-UV CD during the folding of hen egg white lysozyme
-
Chaffotte A.F., Guillou Y., Goldberg M.E. Kinetic resolution of peptide bond and side chain far-UV CD during the folding of hen egg white lysozyme. Biochemistry. 31:1992;9694-9702.
-
(1992)
Biochemistry
, vol.31
, pp. 9694-9702
-
-
Chaffotte, A.F.1
Guillou, Y.2
Goldberg, M.E.3
-
52
-
-
0019890801
-
Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor
-
Kosen P.A., Creighton T.E., Blout E.R. Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor. Biochemistry. 20:1981;5744-5760.
-
(1981)
Biochemistry
, vol.20
, pp. 5744-5760
-
-
Kosen, P.A.1
Creighton, T.E.2
Blout, E.R.3
-
53
-
-
0006925492
-
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
-
Kay L.E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 10663-10665
-
-
Kay, L.E.1
Keifer, P.2
Saarinen, T.3
-
54
-
-
0025210153
-
Complete resonance assignment for the polypeptide backbone of interleukin 1 β using three-dimensional heteronuclear NMR spectroscopy
-
Driscoll P.C., Clore G.M., Marion D., Wingfield P.T., Gronenborn A.M. Complete resonance assignment for the polypeptide backbone of interleukin 1 β using three-dimensional heteronuclear NMR spectroscopy. Biochemistry. 20:1990;3542-3556.
-
(1990)
Biochemistry
, vol.20
, pp. 3542-3556
-
-
Driscoll, P.C.1
Clore, G.M.2
Marion, D.3
Wingfield, P.T.4
Gronenborn, A.M.5
-
56
-
-
0033794319
-
Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
-
Schwarzinger S., Kroon G.J.A., Foss T.R., Wright P.E., Dyson H.J. Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J. Biomol. NMR. 18:2000;43-48.
-
(2000)
J. Biomol. NMR
, vol.18
, pp. 43-48
-
-
Schwarzinger, S.1
Kroon, G.J.A.2
Foss, T.R.3
Wright, P.E.4
Dyson, H.J.5
-
57
-
-
0034836367
-
Sequence-dependent correction of random coil NMR chemical shifts
-
Schwarzinger S., Kroon G.J.A., Foss T.R., Chung J., Wright P.E., Dyson H.J. Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123:2001;2970-2978.
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 2970-2978
-
-
Schwarzinger, S.1
Kroon, G.J.A.2
Foss, T.R.3
Chung, J.4
Wright, P.E.5
Dyson, H.J.6
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