Mapping protein-polymer conformations in bioconjugates with atomic precision
This journal is © The Royal Society of Chemistry 2020..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:11 |
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| Enthalten in: |
Chemical science - 11(2020), 24 vom: 28. Juni, Seite 6160-6166 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Burridge, Kevin M [VerfasserIn] |
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| Anmerkungen: |
Date Revised 12.11.2023 published: Electronic-eCollection Citation Status PubMed-not-MEDLINE |
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| doi: |
10.1039/d0sc02200d |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM31524352X |
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| 520 | |a This journal is © The Royal Society of Chemistry 2020. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 700 | 1 | |a Shurina, Ben A |e verfasserin |4 aut | |
| 700 | 1 | |a Kozuszek, Caleb T |e verfasserin |4 aut | |
| 700 | 1 | |a Parnell, Ryan F |e verfasserin |4 aut | |
| 700 | 1 | |a Montgomery, Jonathan S |e verfasserin |4 aut | |
| 700 | 1 | |a VanPelt, Jamie L |e verfasserin |4 aut | |
| 700 | 1 | |a Daman, Nicholas M |e verfasserin |4 aut | |
| 700 | 1 | |a McCarrick, Robert M |e verfasserin |4 aut | |
| 700 | 1 | |a Ramelot, Theresa A |e verfasserin |4 aut | |
| 700 | 1 | |a Konkolewicz, Dominik |e verfasserin |4 aut | |
| 700 | 1 | |a Page, Richard C |e verfasserin |4 aut | |
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