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38 EguchiT.KuwaharaT.SakuraiM.KomoriT.FujimotoT.ItoG.et al (2018)

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203 While structural details of the apo form are missing for this groups of Cu I sensors, ion mobility mass spectrometry studies on this protein suggest that metal binding subtly alters the shape of the tetramer to a more hydrodynamically compact structure 375 which may lead to changes in the surface electrostatic potential distribution similar to that observed for Sl CsoR

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Such changes are thought to impair the clearance of abnormal protein aggregates