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Issue 24, 2020
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Mapping protein–polymer conformations in bioconjugates with atomic precision

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Abstract

Rational design of protein–polymer bioconjugates is hindered by limited experimental data and mechanistic understanding on interactions between the two. In this communication, nuclear magnetic resonance (NMR) paramagnetic relaxation enhancement (PRE) reports on distances between paramagnetic spin labels and NMR active nuclei, informing on the conformation of conjugated polymers. 1H/15N-heteronuclear single quantum coherence (HSQC) NMR spectra were collected for ubiquitin (Ub) modified with block copolymers incorporating spin labels at different positions along their backbone. The resultant PRE data show that the conjugated polymers have conformations biased towards the nonpolar β-sheet face of Ub, rather than behaving as if in solution. The bioconjugates are stabilized against denaturation by guanidine-hydrochloride, as measured by circular dichroism (CD), and this stabilization is attributed to the interaction between the protein and conjugated polymer.

Graphical abstract: Mapping protein–polymer conformations in bioconjugates with atomic precision

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Supplementary files

Article information


Submitted
17 Apr 2020
Accepted
02 Jun 2020
First published
03 Jun 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2020,11, 6160-6166
Article type
Edge Article

Mapping protein–polymer conformations in bioconjugates with atomic precision

K. M. Burridge, B. A. Shurina, C. T. Kozuszek, R. F. Parnell, J. S. Montgomery, J. L. VanPelt, N. M. Daman, R. M. McCarrick, T. A. Ramelot, D. Konkolewicz and R. C. Page, Chem. Sci., 2020, 11, 6160
DOI: 10.1039/D0SC02200D

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