A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering

Biophysics Reviews
Júlio C BorgesLeandro R S Barbosa

Abstract

Intrinsic flexibility is closely related to protein function, and a plethora of important regulatory proteins have been found to be flexible, multi-domain or even intrinsically disordered. On the one hand, understanding such systems depends on how these proteins behave in solution. On the other, small-angle X-ray scattering (SAXS) is a technique that fulfills the requirements to study protein structure and dynamics relatively quickly with few experimental limitations. Molecular chaperones from Hsp70 and Hsp90 families are multi-domain proteins containing flexible and/or disordered regions that play central roles in cellular proteostasis. Here, we review the structure and function of these proteins by SAXS. Our general approach includes the use of SAXS data to determine size and shape parameters, as well as protein shape reconstruction and their validation by using accessory biophysical tools. Some remarkable examples are presented that exemplify the potential of the SAXS technique. Protein structure can be determined in solution even at limiting protein concentrations (for example, human mortalin, a mitochondrial Hsp70 chaperone). The protein organization, flexibility and function (for example, the J-protein co-chaperones), oli...Continue Reading

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Citations

May 17, 2017·Biophysics Reviews·Cris Dos Remedios
May 3, 2018·Scientific Reports·Yizhi ZhangBrigitte Gontero
Aug 14, 2019·Archives of Biochemistry and Biophysics·Hélène LaunayBrigitte Gontero
Sep 17, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Noeli S M SilvaJúlio C Borges
Jan 4, 2020·International Journal of Biological Macromolecules·Vanessa T R KiralyJúlio C Borges
Sep 28, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Noeli Soares Melo SilvaJúlio César Borges

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