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Abbruzzetti, S., Crema, E., Masino, L., Vecli, A., Viappiani, C., Small, J. R., et al. (2000). Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump. Biophys J, 78(1), 405–415.
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Ballew, R. M., Sabelko, J., & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. U.S.A., 93(12), 5759–5764.
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Chiba, K., Ikai, A., Kawamura-Konishi, Y., & Kihara, H. (1994). Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods. Proteins, 19(2), 110–119.
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Gilmanshin, R., Callender, R. H., & Dyer, R. B. (1998). The core of apomyoglobin E-form folds at the diffusion limit. Nat Struct Biol, 5(5), 363–365.
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Gulotta, M., Gilmanshin, R., Buscher, T. C., Callender, R. H., & Dyer, R. B. (2001). Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape. Biochemistry, 40(17), 5137–5143.
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Gulotta, M., Rogatsky, E., Callender, R. H., & Dyer, R. B. (2003). Primary folding dynamics of sperm whale apomyoglobin: core formation. Biophys J, 84(3), 1909–1918.
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Haruta, N., & Kitagawa, T. (2002). Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin. Biochemistry, 41(21), 6595–6604.
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Miksovska, J., & Larsen, R. W. (2003). Photothermal studies of pH induced unfolding of apomyoglobin. J Protein Chem, 22(4), 387–394.
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Polverini, E., Cugini, G., Annoni, F., Abbruzzetti, S., Viappiani, C., & Gensch, T. (2006). Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red. Biochemistry, 45(16), 5111–5121.
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Reynhout, I. C., Cornelissen, J. J. L. M., & Nolte, R. J. M. (2007). Self-assembled architectures from biohybrid triblock copolymers. J Am Chem Soc, 129(8), 2327–2332.
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