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

ABSTRACT: 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 of sHSPs. However, relationship between the dynamic structure of sHSPs and their chaperone-like activity remains insufficiently characterized. Many factors (temperature, ions, a target protein, crowding etc.) affect the structure and activity of sHSPs. The least studied is an effect of crowding on sHSPs activity. In this work the chaperone-like activity of HSPB5 was quantitatively characterized by dynamic light scattering using two test systems, namely test systems based on heat-induced aggregat

SUBMITTER: Chebotareva NA 

PROVIDER: S-EPMC7404038 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature