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Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues

Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies of the phosphoserine residue (pSer), we address the...

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Autores principales: Rapp, Chaya, Klerman, Hadassa, Levine, Emily, McClendon, Christopher L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3589483/
https://www.ncbi.nlm.nih.gov/pubmed/23472106
http://dx.doi.org/10.1371/journal.pone.0057804
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author Rapp, Chaya
Klerman, Hadassa
Levine, Emily
McClendon, Christopher L.
author_facet Rapp, Chaya
Klerman, Hadassa
Levine, Emily
McClendon, Christopher L.
author_sort Rapp, Chaya
collection PubMed
description Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies of the phosphoserine residue (pSer), we address the distinct nature of hydrogen bonding interactions in phosphotyrosine (pTyr) and sulfotyrosine (sTyr) residues. We derive partial charges for these modified residues and then study them in the context of molecular dynamics simulation of model tripeptides and sulfated protein complexes, potentials of mean force for interacting residue pairs, and a survey of the interactions of modified residues among experimental protein structures. Overall, our findings show that for pTyr, bidentate interactions with Arg are particularly dominant, as has been previously demonstrated for pSer. sTyr interactions with Arg are significantly weaker, even as compared to the same interactions made by the Glu residue. Our work sheds light on the distinct nature of these modified tyrosine residues, and provides a physical-chemical foundation for future studies with the goal of understanding their roles in systems of biological interest.
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spelling pubmed-35894832013-03-07 Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues Rapp, Chaya Klerman, Hadassa Levine, Emily McClendon, Christopher L. PLoS One Research Article Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies of the phosphoserine residue (pSer), we address the distinct nature of hydrogen bonding interactions in phosphotyrosine (pTyr) and sulfotyrosine (sTyr) residues. We derive partial charges for these modified residues and then study them in the context of molecular dynamics simulation of model tripeptides and sulfated protein complexes, potentials of mean force for interacting residue pairs, and a survey of the interactions of modified residues among experimental protein structures. Overall, our findings show that for pTyr, bidentate interactions with Arg are particularly dominant, as has been previously demonstrated for pSer. sTyr interactions with Arg are significantly weaker, even as compared to the same interactions made by the Glu residue. Our work sheds light on the distinct nature of these modified tyrosine residues, and provides a physical-chemical foundation for future studies with the goal of understanding their roles in systems of biological interest. Public Library of Science 2013-03-05 /pmc/articles/PMC3589483/ /pubmed/23472106 http://dx.doi.org/10.1371/journal.pone.0057804 Text en © 2013 Rapp et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Rapp, Chaya
Klerman, Hadassa
Levine, Emily
McClendon, Christopher L.
Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title_full Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title_fullStr Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title_full_unstemmed Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title_short Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
title_sort hydrogen bond strengths in phosphorylated and sulfated amino acid residues
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3589483/
https://www.ncbi.nlm.nih.gov/pubmed/23472106
http://dx.doi.org/10.1371/journal.pone.0057804
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