A modified Ising model for the thermodynamic properties of local and global protein folding–unfolding observed by circular dichroism and small-angle X-ray scattering

Shiu, Y.-J.; Jeng, U.-S.; Su, C.; Huang, Y.-S.; Hayashi, M.; Liang, K.-K.; Yeh, Y.-L.; Lin, S.-H.

doi:10.1107/S0021889807003597

Journal of Applied Crystallography Journal of Applied
Crystallography

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Figure 1
The simulated Obs(m) for a protein consisting of two groups. Given in (a) are the profiles simulated with three $[\Delta \Delta \varepsilon ^{(2)}]$ values of −3.0k_BT (solid line), −1.5k_BT (dashed line), and −1.2 k_BT (dotted line), with fixed $[\Delta \Delta \varepsilon ^{(1)} = - 1.0k_{\rm B}T]$ and equal weighting parameters of $[\gamma ^{(1)} = \gamma ^{(2)} = 0.5]$ . (b) The last case in (a) (solid circles), contributed from f_u⁽¹⁾ (m) (circles) and f_u⁽²⁾ (m) (triangles) of the two groups of close free energies, is approximated by the Obs(m) of one reduced group (solid line).

JOURNAL OF
APPLIED
CRYSTALLOGRAPHY

ISSN: 1600-5767

Volume 40| Part s1| February 2007| Pages s195-s199

doi:10.1107/S0021889807003597

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