The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy
The primary sequence of antifreeze glycoproteins (AFGPs) is highly degenerate, consisting of multiple repeats of the same tripeptide, Ala–Ala–Thr*, in which Thr* is a glycosylated threonine with the disaccharide beta-d-galactosyl-(1,3)-alpha-N-acetyl-d-galactosamine. AFGPs seem to function as intrin...
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ftmdpi:oai:mdpi.com:/2218-273X/9/6/235/ 2023-08-20T04:02:34+02:00 The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy Cheenou Her Yin Yeh Viswanathan V. Krishnan agris 2019-06-17 application/pdf https://doi.org/10.3390/biom9060235 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/biom9060235 https://creativecommons.org/licenses/by/4.0/ Biomolecules; Volume 9; Issue 6; Pages: 235 AFGP NMR ensemble of structures antifreeze proteins Text 2019 ftmdpi https://doi.org/10.3390/biom9060235 2023-07-31T22:21:54Z The primary sequence of antifreeze glycoproteins (AFGPs) is highly degenerate, consisting of multiple repeats of the same tripeptide, Ala–Ala–Thr*, in which Thr* is a glycosylated threonine with the disaccharide beta-d-galactosyl-(1,3)-alpha-N-acetyl-d-galactosamine. AFGPs seem to function as intrinsically disordered proteins, presenting challenges in determining their native structure. In this work, a different approach was used to elucidate the three-dimensional structure of AFGP8 from the Arctic cod Boreogadus saida and the Antarctic notothenioid Trematomus borchgrevinki. Dimethyl sulfoxide (DMSO), a non-native solvent, was used to make AFGP8 less dynamic in solution. Interestingly, DMSO induced a non-native structure, which could be determined via nuclear magnetic resonance (NMR) spectroscopy. The overall three-dimensional structures of the two AFGP8s from two different natural sources were different from a random coil ensemble, but their “compactness” was very similar, as deduced from NMR measurements. In addition to their similar compactness, the conserved motifs, Ala–Thr*–Pro–Ala and Ala–Thr*–Ala–Ala, present in both AFGP8s, seemed to have very similar three-dimensional structures, leading to a refined definition of local structural motifs. These local structural motifs allowed AFGPs to be considered functioning as effectors, making a transition from disordered to ordered upon binding to the ice surface. In addition, AFGPs could act as dynamic linkers, whereby a short segment folds into a structural motif, while the rest of the AFGPs could still be disordered, thus simultaneously interacting with bulk water molecules and the ice surface, preventing ice crystal growth. Text Antarc* Antarctic Arctic cod Arctic Boreogadus saida MDPI Open Access Publishing Arctic Antarctic The Antarctic Biomolecules 9 6 235 |
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ftmdpi |
language |
English |
topic |
AFGP NMR ensemble of structures antifreeze proteins |
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AFGP NMR ensemble of structures antifreeze proteins Cheenou Her Yin Yeh Viswanathan V. Krishnan The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
topic_facet |
AFGP NMR ensemble of structures antifreeze proteins |
description |
The primary sequence of antifreeze glycoproteins (AFGPs) is highly degenerate, consisting of multiple repeats of the same tripeptide, Ala–Ala–Thr*, in which Thr* is a glycosylated threonine with the disaccharide beta-d-galactosyl-(1,3)-alpha-N-acetyl-d-galactosamine. AFGPs seem to function as intrinsically disordered proteins, presenting challenges in determining their native structure. In this work, a different approach was used to elucidate the three-dimensional structure of AFGP8 from the Arctic cod Boreogadus saida and the Antarctic notothenioid Trematomus borchgrevinki. Dimethyl sulfoxide (DMSO), a non-native solvent, was used to make AFGP8 less dynamic in solution. Interestingly, DMSO induced a non-native structure, which could be determined via nuclear magnetic resonance (NMR) spectroscopy. The overall three-dimensional structures of the two AFGP8s from two different natural sources were different from a random coil ensemble, but their “compactness” was very similar, as deduced from NMR measurements. In addition to their similar compactness, the conserved motifs, Ala–Thr*–Pro–Ala and Ala–Thr*–Ala–Ala, present in both AFGP8s, seemed to have very similar three-dimensional structures, leading to a refined definition of local structural motifs. These local structural motifs allowed AFGPs to be considered functioning as effectors, making a transition from disordered to ordered upon binding to the ice surface. In addition, AFGPs could act as dynamic linkers, whereby a short segment folds into a structural motif, while the rest of the AFGPs could still be disordered, thus simultaneously interacting with bulk water molecules and the ice surface, preventing ice crystal growth. |
format |
Text |
author |
Cheenou Her Yin Yeh Viswanathan V. Krishnan |
author_facet |
Cheenou Her Yin Yeh Viswanathan V. Krishnan |
author_sort |
Cheenou Her |
title |
The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
title_short |
The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
title_full |
The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
title_fullStr |
The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
title_full_unstemmed |
The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy |
title_sort |
ensemble of conformations of antifreeze glycoproteins (afgp8): a study using nuclear magnetic resonance spectroscopy |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
https://doi.org/10.3390/biom9060235 |
op_coverage |
agris |
geographic |
Arctic Antarctic The Antarctic |
geographic_facet |
Arctic Antarctic The Antarctic |
genre |
Antarc* Antarctic Arctic cod Arctic Boreogadus saida |
genre_facet |
Antarc* Antarctic Arctic cod Arctic Boreogadus saida |
op_source |
Biomolecules; Volume 9; Issue 6; Pages: 235 |
op_relation |
https://dx.doi.org/10.3390/biom9060235 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/biom9060235 |
container_title |
Biomolecules |
container_volume |
9 |
container_issue |
6 |
container_start_page |
235 |
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1774713081812746240 |