Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins

Noritaka Nishida; Maho Yagi-Utsumi; Fumihiro Motojima; Masasuke Yoshida; Ichio Shimada; Koichi Kato

doi:10.1016/j.jbiosc.2013.02.012

Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins

J Biosci Bioeng. 2013 Aug;116(2):160-4. doi: 10.1016/j.jbiosc.2013.02.012. Epub 2013 Apr 6.

Authors

Noritaka Nishida¹, Maho Yagi-Utsumi, Fumihiro Motojima, Masasuke Yoshida, Ichio Shimada, Koichi Kato

Affiliation

¹ Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

PMID: 23567152
DOI: 10.1016/j.jbiosc.2013.02.012

Abstract

GroEL-protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largely unfolded and highly mobile, enabling identification of the interaction hot spots displayed on intrinsically disordered proteins.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Binding Sites
Cattle
Chaperonin 60 / chemistry
Chaperonin 60 / metabolism*
Intrinsically Disordered Proteins / chemistry*
Intrinsically Disordered Proteins / metabolism
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Thiosulfate Sulfurtransferase / chemistry
Thiosulfate Sulfurtransferase / metabolism
alpha-Synuclein / chemistry
alpha-Synuclein / metabolism

Substances

Chaperonin 60
Intrinsically Disordered Proteins
alpha-Synuclein
Thiosulfate Sulfurtransferase