Work

SPR spectroscopic analysis of myosin binding to wild type and mutant UNC45B

Year: 2024

Type: article

Abstract: UNC45B is a multidomain molecular chaperone that is essential for the proper folding and function of myosin. It has previously been demonstrated that the UCS domain is responsible for the chaperoning function of UNC45B and that removing its client-binding loop leads to a significant change in its solution conformation and a reduced chaperoning function. Here, we report the direct quantification of affinities of myosin binding to wild type and mutant UNC45B using surface plasmon resonance (SPR) spectroscopy. We found that deletion of the client-binding loop in UNC45B resulted in a dramatic decrease in myosin affinity.

Source: PubMed

DOI: 10.17912/micropub.biology.001131

Authors: Silvana Valdebenito, Eliseo Eugenin, Andres Oberhauser

Institution: The University of Texas Medical Branch at Galveston

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institutes of Health

Award: G9000014034