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Surface Accessibility of an Intrinsically Disordered Protein Probed by 2D Time-Resolved Laser-Assisted NMR Spectroscopy

Cited 1 time in Web of Science Cited 1 time in Scopus
Authors

Im, Jonghyuk; Lee, Jongchan; Lee, Jung Ho

Issue Date
2022-09
Publisher
American Chemical Society
Citation
Journal of the American Chemical Society, Vol.144 No.37, pp.17010-17021
Abstract
Probing the protein surface accessibility of different residues is a powerful way of characterizing the overall conformation of intrinsically disordered proteins (IDPs). We present a two-dimensional (2D) time-resolved photo-CIDNP (TR-CIDNP) experiment suitable for IDP analysis. Pulse stretching of high-power laser pulses, band-selective decoupling of( 13)C(alpha), and simultaneous application of radiofrequency and laser pulses were implemented to quantitatively analyze the IDP surface at ultrahigh resolution. Comparative analysis with other methods that measure protein surface accessibility validated the newly developed method and emphasized the importance of dye charge in photo-CIDNP. Using the neutral riboflavin dye, surface accessibilities were measured to be nearly identical for the four Tyr residues of alpha-synuclein (alpha-Syn), whose H-1(alpha)-C-13(alpha) correlations were well-resolved in the 2D TR-CIDNP spectrum. Having confirmed the similarity between the time-resolved and steady-state photo-CIDNP results for alpha-Syn, we used the more sensitive latter method to show that divalent cations induce compaction of the C-terminal region and release of the N-terminal region of alpha-Syn. The photo-CIDNP method presented herein can be used as an orthogonal and independent method for investigating important biological processes associated with changes in the overall IDP conformation.
ISSN
0002-7863
URI
https://hdl.handle.net/10371/186584
DOI
https://doi.org/10.1021/jacs.2c06309
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