Design of buried charged networks in artificial proteins
Buried charged networks in proteins are often important for their biological functionality and are believed to destabilise the protein fold. Here, the authors combine computational design, MD simulations, biophysical experiments, NMR and X-ray crystallography to design and characterise artificial 4α...
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Nature Portfolio
2021
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oai:doaj.org-article:0e77cdff4a874a32b8c39f0694e34a3c2021-12-02T14:02:51ZDesign of buried charged networks in artificial proteins10.1038/s41467-021-21909-72041-1723https://doaj.org/article/0e77cdff4a874a32b8c39f0694e34a3c2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21909-7https://doaj.org/toc/2041-1723Buried charged networks in proteins are often important for their biological functionality and are believed to destabilise the protein fold. Here, the authors combine computational design, MD simulations, biophysical experiments, NMR and X-ray crystallography to design and characterise artificial 4α-helical proteins with buried charged elements. They analyse their conformational landscapes and observe that the ion-pairs are stabilised by amphiphilic residues that electrostatically shield the charged motif, which increases structural stability.Mona BaumgartMichael RöpkeMax E. MühlbauerSam AsamiSophie L. MaderKai FredrikssonMichael GrollAna P. Gamiz-HernandezVille R. I. KailaNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021) |
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Science Q Mona Baumgart Michael Röpke Max E. Mühlbauer Sam Asami Sophie L. Mader Kai Fredriksson Michael Groll Ana P. Gamiz-Hernandez Ville R. I. Kaila Design of buried charged networks in artificial proteins |
description |
Buried charged networks in proteins are often important for their biological functionality and are believed to destabilise the protein fold. Here, the authors combine computational design, MD simulations, biophysical experiments, NMR and X-ray crystallography to design and characterise artificial 4α-helical proteins with buried charged elements. They analyse their conformational landscapes and observe that the ion-pairs are stabilised by amphiphilic residues that electrostatically shield the charged motif, which increases structural stability. |
format |
article |
author |
Mona Baumgart Michael Röpke Max E. Mühlbauer Sam Asami Sophie L. Mader Kai Fredriksson Michael Groll Ana P. Gamiz-Hernandez Ville R. I. Kaila |
author_facet |
Mona Baumgart Michael Röpke Max E. Mühlbauer Sam Asami Sophie L. Mader Kai Fredriksson Michael Groll Ana P. Gamiz-Hernandez Ville R. I. Kaila |
author_sort |
Mona Baumgart |
title |
Design of buried charged networks in artificial proteins |
title_short |
Design of buried charged networks in artificial proteins |
title_full |
Design of buried charged networks in artificial proteins |
title_fullStr |
Design of buried charged networks in artificial proteins |
title_full_unstemmed |
Design of buried charged networks in artificial proteins |
title_sort |
design of buried charged networks in artificial proteins |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/0e77cdff4a874a32b8c39f0694e34a3c |
work_keys_str_mv |
AT monabaumgart designofburiedchargednetworksinartificialproteins AT michaelropke designofburiedchargednetworksinartificialproteins AT maxemuhlbauer designofburiedchargednetworksinartificialproteins AT samasami designofburiedchargednetworksinartificialproteins AT sophielmader designofburiedchargednetworksinartificialproteins AT kaifredriksson designofburiedchargednetworksinartificialproteins AT michaelgroll designofburiedchargednetworksinartificialproteins AT anapgamizhernandez designofburiedchargednetworksinartificialproteins AT villerikaila designofburiedchargednetworksinartificialproteins |
_version_ |
1718392065093533696 |