New insight into the dynamical system of αB-crystallin oligomers
Abstract
α-Crystallin possesses a dynamic quaternary structure mediated by its subunit dynamics. Elucidation of a mechanism of subunit dynamics in homo-oligomers of αB-crystallin was tackled through deuteration-assisted small-angle neutron scattering (DA-SANS) and electrospray ionization (ESI) native mass spectrometry (nMS). The existence of subunit exchange was confirmed with DA-SANS, and monomers liberated from the oligomers were observed with nMS. With increasing temperature, an increase in both the exchange rate and monomer population was observed despite the absence of oligomer collapse. It is proposed that transiently liberated subunits, namely, “traveling subunits, ” play a role in subunit exchange. Moreover, we propose that protein function is regulated by these traveling subunits.
Journal
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- Scientific Reports
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Scientific Reports 6 2016-07-06
Springer Nature
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Keywords
Details 詳細情報について
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- CRID
- 1050001335849291648
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- NII Article ID
- 120006323745
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- ISSN
- 20452322
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- HANDLE
- 2433/226356
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- CiNii Articles