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. 2010 Sep 29;11(10):3725–3747. doi: 10.3390/ijms11103725

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© 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Disorder prediction and sequence alignment for proteins in Table 2, which are reverse alignment matches of all the MoRF regions of three proteins. The alignment was also cut off at E-value of 0.001. Disorder scores were predicted by PONDR®VL-XT. In the insets of sequence alignment, the sequential order of original MoRF regions were shown in a reversed order, while other alignment hits were shown in normal sequential order. The curves of disorder score were also shifted to allowed the overlapped of aligned segments. N, C1, C2, and C4 MoRF regions of RNase E were shown in (a)–(d), accordingly. C1 MoRF region of P53 was presented in (e). N, M1, M2, and C2 MoRF regions of SRC-3 were plotted in (e)–(i), respectively.

Disorder prediction and sequence alignment for proteins in Table 2, which are reverse alignment matches of all the MoRF regions of three proteins. The alignment was also cut off at E-value of 0.001. Disorder scores were predicted by PONDR®VL-XT. In the insets of sequence alignment, the sequential order of original MoRF regions were shown in a reversed order, while other alignment hits were shown in normal sequential order. The curves of disorder score were also shifted to allowed the overlapped of aligned segments. N, C1, C2, and C4 MoRF regions of RNase E were shown in (a)–(d), accordingly. C1 MoRF region of P53 was presented in (e). N, M1, M2, and C2 MoRF regions of SRC-3 were plotted in (e)–(i), respectively.

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