Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding

Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding

Small heat-shock proteins (sHSPs) are ATP-independent molecular chaperones that interact with partially unfolded proteins, preventing their aberrant aggregation, thereby exhibiting a chaperone-like activity. Dynamics of the quaternary structure plays an important role in the chaperone-like activity...

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Bibliographic Details
Main Authors: Natalia A. Chebotareva, Svetlana G. Roman, Vera A. Borzova, Tatiana B. Eronina, Valeriya V. Mikhaylova, Boris I. Kurganov
Format: Article
Language:English
Published: MDPI AG 2020-07-01
Series:International Journal of Molecular Sciences
Subjects:
HSPB5
chaperone-like activity
oligomeric states
mixed crowding
Online Access:https://www.mdpi.com/1422-0067/21/14/4940

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https://www.mdpi.com/1422-0067/21/14/4940

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