List View
 |   | 
Author (up) Title Year Publication Serial Volume Pages
Ballew, R.M.; Sabelko, J.; Gruebele, M. Direct observation of fast protein folding: the initial collapse of apomyoglobin 1996 Proceedings of the National Academy of Sciences of the United States of America 3798 93 5759-5764
Bayley, P.; Martin, S.; Anson, M. Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution 1975 Biochemical and Biophysical Research Communications 3816 66 303-308
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods 1994 Proteins 3799 19 110-119
Haruta, N.; Kitagawa, T. Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin 2002 Biochemistry 3785 41 6595-6604
Hasumi, H. Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method 1980 Biochimica et Biophysica Acta 3876 626 265-276
Miksovska, J.; Larsen, R.W. Photothermal studies of pH induced unfolding of apomyoglobin 2003 Journal of Protein Chemistry 3780 22 387-394
Uzawa, T.; Akiyama, S.; Kimura, T.; Takahashi, S.; Ishimori, K.; Morishima, I.; Fujisawa, T. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness 2004 Proceedings of the National Academy of Sciences of the United States of America 3779 101 1171-1176