Design of buried charged networks in artificial proteins

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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Main Authors: Mona Baumgart, Michael Röpke, Max E. Mühlbauer, Sam Asami, Sophie L. Mader, Kai Fredriksson, Michael Groll, Ana P. Gamiz-Hernandez, Ville R. I. Kaila
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21909-7
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spelling doaj-0e77cdff4a874a32b8c39f0694e34a3c2021-03-28T11:13:00ZengNature Publishing GroupNature Communications2041-17232021-03-011211910.1038/s41467-021-21909-7Design of buried charged networks in artificial proteinsMona Baumgart0Michael Röpke1Max E. Mühlbauer2Sam Asami3Sophie L. Mader4Kai Fredriksson5Michael Groll6Ana P. Gamiz-Hernandez7Ville R. I. Kaila8Center for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität MünchenBuried 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.https://doi.org/10.1038/s41467-021-21909-7
collection DOAJ
language English
format Article
sources DOAJ
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
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-03-01
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.
url https://doi.org/10.1038/s41467-021-21909-7
work_keys_str_mv AT monabaumgart designofburiedchargednetworksinartificialproteins
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