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Comment
. 2018 Jun 19;114(12):2757-2758.
doi: 10.1016/j.bpj.2018.05.019.

Tuning Free Energy by Backbone Conformational Entropy: A Strategy from Disordered Proteins

Chia-En A Chang  1
Affiliations
Comment

Tuning Free Energy by Backbone Conformational Entropy: A Strategy from Disordered Proteins

Chia-En A Chang. Biophys J. .
No abstract available

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Figures

Figure 1
Figure 1
Schematic figure describing a protein with an intrinsically disordered region, showing two significantly different backbone conformations but with similar computed conformational entropies. The end-to-end distance of the disordered region is 40 Å (left) and 10 Å (right), and the computed conformational entropy S is ∼64 cal/mol/K for Gly15 by the mutual information expansion (MIE) method (3). To see this figure in color, go online.
See this image and copyright information in PMC

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References

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