Journal
BIOPHYSICAL JOURNAL
Volume 109, Issue 6, Pages 1240-1250Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2015.08.009
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Funding
- Engineering and Physical Sciences Research Council
- Engineering and Physical Sciences Research Council [EP/H051759/1] Funding Source: researchfish
- EPSRC [EP/H051759/1] Funding Source: UKRI
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We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplitude modulation of the thermal fluctuations of the elastic normal modes conveys the allosteric signal, and address the question of what an allosteric pathway means in this case. We find that a perturbation theory of thermal elastic solids and non-perturbative approach (by super-coarse-graining elasticity into internal bending modes) have opposite signatures in their structure of correlated pathways. We illustrate the effect from analysis of previous results from GlxR of Corynebacterium glutamicum, an example of the CRP/FNR transcription family of allosteric homodimers. We find that the visibility of both correlated pathways and disconnected sites of correlated motion in this protein suggests that mechanisms of local elastic stretch and bend are recruited for the purpose of creating and controlling allosteric cooperativity.
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