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Review
. 1999 Aug 31;96(18):9970-2.
doi: 10.1073/pnas.96.18.9970.

Folding and binding cascades: shifts in energy landscapes

C J Tsai, B Ma, R Nussinov
Review

Folding and binding cascades: shifts in energy landscapes

C J Tsai et al. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
At the bottom of a folding funnel (shown enclosed by a small circle, which is projected and magnified in the larger circle), there are many distinctive, accessible conformations around the most populated native structure. For clarity, only the native structure and the functional conformation are highlighted in the figure. They are indicated by the schematic drawings as Na and Fa, respectively. The conformational change responsible for the cascade reaction in binding is drawn opposite to the binding site to reflect that it is remote from the binding site. On binding (indicated by a dashed rectangle), the environment changes. The change in the environment has the effect of making the folding energy surface shift, to favor the functional conformation (Fb) instead of the native structure (Nb). Hence, in terms of the free energy landscape theory, the functional switch-on mechanism is not by induced and propagated conformational change of the protein molecule through binding; rather, it is a shift of the population toward the functional conformer.
Figure 2
Figure 2
(A). The traditional view of induced fit and allostery where binding in one site (shaded) causes changes at a remote site (rugged). (B) The concept of conformational substates described here, where preexisting conformations are in equilibrium. The equilibrium shifts to one of conformations that fits incoming ligand.
See this image and copyright information in PMC

Comment on

References

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    1. Tsai C J, Kumar S, Ma B, Nussinov R. Protein Sci. 1999;8:1181–1190. - PMC - PubMed

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