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DOI: http://dx.doi.org/10.7554/eLife.06792.015 Our model of PhoQ activation and repression has similarities to a recently proposed two-state computational model in which the PD is predicted to experience broad conformational changes within the periplasmic dimerization interface and acidic patch (Molnar et al., 2014).
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Within these molecular machines, cycles of nucleotide binding and hydrolysis induce conformational changes that affect a broad range of substrate proteins [11,12].
The large conformational changes exhibited by ecDHFR lead to a broad spectrum of active site electrostatic environments that can have substantial effects on the energy landscapes of enzymatic processes.
The conformational changes experimentally observed in the enzymes by binding a broad range of ligands can be predicted by the most cooperative lowest frequency modes of motion by ANM, where the hinges are the key mechanistic regions of the structure that control the conformational ensemble.
Conformational changes were monitored by Raman spectroscopy.
The conformational changes after adsorption are studied.
Protein molecules often undergo conformational changes.
Both homodimers and heterodimers undergo conformational changes upon activation.
Necessarily, the proteasome undergoes large conformational changes during its operation.
This neglects the conformational changes induced by ligand.
Critical elements for the conformational changes are indicated.
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