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. 2002 Oct;11(10):2297–2307. doi: 10.1110/ps.0213102

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Copyright © Copyright 2002 The Protein Society

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Fig. 5. — Free energy landscapes at 300 K drawn by the conventional arbitrary axes. (a) The radius of gyration r_G and the r.m.s.d. from the ordered conformation, (b) the hydrophobic ASA and the r.m.s.d., and (c) r_G and the numbers of kHB were used. The contour value in kcal/mol is shown on the right side of the figure. The double circles on the axis at r.m.s.d. = 0 are the positions for the ordered conformation. White and pink dots are the transition state conformations at A ― E and at B ― E in Fig. 1b ▶, respectively.

Fig. 5. — Free energy landscapes at 300 K drawn by the conventional arbitrary axes. (a) The radius of gyration r_G and the r.m.s.d. from the ordered conformation, (b) the hydrophobic ASA and the r.m.s.d., and (c) r_G and the numbers of kHB were used. The contour value in kcal/mol is shown on the right side of the figure. The double circles on the axis at r.m.s.d. = 0 are the positions for the ordered conformation. White and pink dots are the transition state conformations at A ― E and at B ― E in Fig. 1b ▶, respectively.