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

Paper ID Volume ID Publish Year Pages File Format Full-Text
20614 43183 2013 5 PDF Available
Title
Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins
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.

Keywords
GroEL; Nuclear magnetic resonance; Molecular chaperone; Intrinsically disordered protein; Rhodanese; α-Synuclein; DenaturationαSN, α-synuclein; DTT, dithiothreitol; GdmCl, guanidium chloride; HSQC, heteronuclear single-quantum coherence; Rho, rhodanese; S
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Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 116, Issue 2, August 2013, Pages 160–164
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us