Hidden information on protein function in censuses of proteome foldedness

Dezerae Cox; Ching-Seng Ang; Nadinath B. Nillegoda; Gavin E. Reid; Danny M. Hatters

doi:10.1038/s41467-022-29661-2

Nature Communications (Apr 2022)

Hidden information on protein function in censuses of proteome foldedness

Dezerae Cox,
Ching-Seng Ang,
Nadinath B. Nillegoda,
Gavin E. Reid,
Danny M. Hatters

Affiliations

Dezerae Cox: Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne
Ching-Seng Ang: Melbourne Mass Spectrometry and Proteomics Facility, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne
Nadinath B. Nillegoda: Australian Regenerative Medicine Institute, Monash University
Gavin E. Reid: Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne
Danny M. Hatters: Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne

DOI: https://doi.org/10.1038/s41467-022-29661-2
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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Proteomics can define features of proteome foldedness by assessing the reactivity of surface exposed amino acids. Here, the authors show that such exposure patterns yield insight to structural changes in chaperones as they bind to unfolded proteins in urea-denatured mammalian cell lysate.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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