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G. V ANDERHEEREN and I. HANSSENS: The Perception of Hydrophobic Clusters
References
Acharya KR, Stuart DI, Walker NPC, Lewis M, Philips DC (1989) Refined structure of baboon
a-lactalbumin at 1.7 A resolution. J Mol Bioi 208: 99-127.
Coco MJ, Lecomte JT (1994) The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent probe ANS. Protein
Sci 3: 267-281.
Engelhard M, Evans PA (1995) Kinetics of interaction of partially folded proteins with a hydrophobic
dye: evidence that the molten globule character is maximal in early folding intermediates. Protein
Sci 4: 1553-1562.
Das KP, Surewicz WK (1995) Temperature induced exposure of hydrophobic surfaces and its effect on
the chaperone activity of a-Crystallin. FEBS Lett 369: 321-325.
Gorovits BM, Seale JW, Horowitz PM (1995) Residual structure in urea-denaturated chaperonin
GroEL. Biochemistry 34: 13928-13933.
Levitt M, Goestein M, Huang E, Subbiah S, Tsai J (1997) Protein folding: the endgame. Ann Rev
Biochem 66: 549-579.
Miranker AD, Dobson CD (1996) Collapse and cooperativity in protein folding. Curr Opin Struct Bioi
6:31-42.
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI (1990) Evidence for a molten globule
state as a general intermediate state in protein folding. FEBS Lett 262: 20-24.
Seale WS, Martinez JL, Horowitz PM (1995) Photoincorporation of 4,4'-bis(l-anilino-8naphthalenesulfonic acid) into the apical domain of GroEL. Biochemistry 35: 7443-7449.
Shi L, Palleros DR, Fink AL (1994) Protein conformational change induced by 1,1'-bis(4-anilino-5naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 33:
7536-7546.
Stuart DI, Acharya KR, Walker NPC, Smith SG, Lewis M, Phillips DC (1986) a-lactalbumin possesses
a novel calcium binding loop. Nature 324: 84-87.
Teschke CM, King J, Prevelige PE (l993) Folding of the phage P22 coat protein in vitro. Biochemistry
32: 10839-10847.
Vanderheeren G, Hanssens I (1994) Thermal unfolding of bovine a-lactalbumin. Comparison of circular dichroism with hydrophobicity measurements. J Bioi Chern 269: 7090-7094.
Vanderheeren G, Hanssens I, Noyelle K, Van Dael H, Joniau M (1998) The perturbations of the native
state of goat a-lactalbumin induced by 1,1'-bis(4-anilino-5-naphthalenesulfonate) are Ca2+_
dependent. Biophys J 75: 2195-2204.
Ward LD, TimasheffSN (1994) Cooperative multiple binding ofbis-ANS and daunomycin to tubulin.
Biochemistry 33: 11891-11899.
G. V ANDERHEEREN and I. HANSSENS: The Perception of Hydrophobic Clusters
References
Acharya KR, Stuart DI, Walker NPC, Lewis M, Philips DC (1989) Refined structure of baboon
a-lactalbumin at 1.7 A resolution. J Mol Bioi 208: 99-127.
Coco MJ, Lecomte JT (1994) The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent probe ANS. Protein
Sci 3: 267-281.
Engelhard M, Evans PA (1995) Kinetics of interaction of partially folded proteins with a hydrophobic
dye: evidence that the molten globule character is maximal in early folding intermediates. Protein
Sci 4: 1553-1562.
Das KP, Surewicz WK (1995) Temperature induced exposure of hydrophobic surfaces and its effect on
the chaperone activity of a-Crystallin. FEBS Lett 369: 321-325.
Gorovits BM, Seale JW, Horowitz PM (1995) Residual structure in urea-denaturated chaperonin
GroEL. Biochemistry 34: 13928-13933.
Levitt M, Goestein M, Huang E, Subbiah S, Tsai J (1997) Protein folding: the endgame. Ann Rev
Biochem 66: 549-579.
Miranker AD, Dobson CD (1996) Collapse and cooperativity in protein folding. Curr Opin Struct Bioi
6:31-42.
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI (1990) Evidence for a molten globule
state as a general intermediate state in protein folding. FEBS Lett 262: 20-24.
Seale WS, Martinez JL, Horowitz PM (1995) Photoincorporation of 4,4'-bis(l-anilino-8naphthalenesulfonic acid) into the apical domain of GroEL. Biochemistry 35: 7443-7449.
Shi L, Palleros DR, Fink AL (1994) Protein conformational change induced by 1,1'-bis(4-anilino-5naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 33:
7536-7546.
Stuart DI, Acharya KR, Walker NPC, Smith SG, Lewis M, Phillips DC (1986) a-lactalbumin possesses
a novel calcium binding loop. Nature 324: 84-87.
Teschke CM, King J, Prevelige PE (l993) Folding of the phage P22 coat protein in vitro. Biochemistry
32: 10839-10847.
Vanderheeren G, Hanssens I (1994) Thermal unfolding of bovine a-lactalbumin. Comparison of circular dichroism with hydrophobicity measurements. J Bioi Chern 269: 7090-7094.
Vanderheeren G, Hanssens I, Noyelle K, Van Dael H, Joniau M (1998) The perturbations of the native
state of goat a-lactalbumin induced by 1,1'-bis(4-anilino-5-naphthalenesulfonate) are Ca2+_
dependent. Biophys J 75: 2195-2204.
Ward LD, TimasheffSN (1994) Cooperative multiple binding ofbis-ANS and daunomycin to tubulin.
Biochemistry 33: 11891-11899.