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Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H
Surfactant proteins are well known from the human lung where they are responsible for the stability and flexibility of the pulmonary surfactant system. They are able to influence the surface tension of the gas–liquid interface specifically by directly interacting with single lipids. This work descri...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101549/ https://www.ncbi.nlm.nih.gov/pubmed/25381619 http://dx.doi.org/10.1007/s00894-014-2513-0 |
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author | Rausch, Felix Schicht, Martin Bräuer, Lars Paulsen, Friedrich Brandt, Wolfgang |
author_facet | Rausch, Felix Schicht, Martin Bräuer, Lars Paulsen, Friedrich Brandt, Wolfgang |
author_sort | Rausch, Felix |
collection | PubMed |
description | Surfactant proteins are well known from the human lung where they are responsible for the stability and flexibility of the pulmonary surfactant system. They are able to influence the surface tension of the gas–liquid interface specifically by directly interacting with single lipids. This work describes the generation of reliable protein structure models to support the experimental characterization of two novel putative surfactant proteins called SP-G and SP-H. The obtained protein models were complemented by predicted posttranslational modifications and placed in a lipid model system mimicking the pulmonary surface. Molecular dynamics simulations of these protein-lipid systems showed the stability of the protein models and the formation of interactions between protein surface and lipid head groups on an atomic scale. Thereby, interaction interface and strength seem to be dependent on orientation and posttranslational modification of the protein. The here presented modeling was fundamental for experimental localization studies and the simulations showed that SP-G and SP-H are theoretically able to interact with lipid systems and thus are members of the surfactant protein family. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00894-014-2513-0) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7101549 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-71015492020-03-31 Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H Rausch, Felix Schicht, Martin Bräuer, Lars Paulsen, Friedrich Brandt, Wolfgang J Mol Model Original Paper Surfactant proteins are well known from the human lung where they are responsible for the stability and flexibility of the pulmonary surfactant system. They are able to influence the surface tension of the gas–liquid interface specifically by directly interacting with single lipids. This work describes the generation of reliable protein structure models to support the experimental characterization of two novel putative surfactant proteins called SP-G and SP-H. The obtained protein models were complemented by predicted posttranslational modifications and placed in a lipid model system mimicking the pulmonary surface. Molecular dynamics simulations of these protein-lipid systems showed the stability of the protein models and the formation of interactions between protein surface and lipid head groups on an atomic scale. Thereby, interaction interface and strength seem to be dependent on orientation and posttranslational modification of the protein. The here presented modeling was fundamental for experimental localization studies and the simulations showed that SP-G and SP-H are theoretically able to interact with lipid systems and thus are members of the surfactant protein family. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00894-014-2513-0) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2014-11-09 2014 /pmc/articles/PMC7101549/ /pubmed/25381619 http://dx.doi.org/10.1007/s00894-014-2513-0 Text en © Springer-Verlag Berlin Heidelberg 2014 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Original Paper Rausch, Felix Schicht, Martin Bräuer, Lars Paulsen, Friedrich Brandt, Wolfgang Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title | Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title_full | Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title_fullStr | Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title_full_unstemmed | Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title_short | Protein modeling and molecular dynamics simulation of the two novel surfactant proteins SP-G and SP-H |
title_sort | protein modeling and molecular dynamics simulation of the two novel surfactant proteins sp-g and sp-h |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101549/ https://www.ncbi.nlm.nih.gov/pubmed/25381619 http://dx.doi.org/10.1007/s00894-014-2513-0 |
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