Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study
dc.contributor.author | Lee, Hui Sun | |
dc.contributor.author | Qi, Yifei | |
dc.contributor.author | Im, Wonpil | |
dc.date.accessioned | 2015-06-16T19:41:32Z | |
dc.date.available | 2015-06-16T19:41:32Z | |
dc.date.issued | 2015-03-09 | |
dc.identifier.citation | Lee, Hui Sun, Yifei Qi, and Wonpil Im. "Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study." Sci Rep. 2015; 5: 8926. http://dx.doi.org/10.1038/srep08926. | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/18078 | |
dc.description.abstract | N-linked glycosylation is one of the most important, chemically complex, and ubiquitous post-translational modifications in all eukaryotes. The N-glycans that are covalently linked to proteins are involved in numerous biological processes. There is considerable interest in developments of general approaches to predict the structural consequences of site-specific glycosylation and to understand how these effects can be exploited in protein design with advantageous properties. In this study, the impacts of N-glycans on protein structure and dynamics are systematically investigated using an integrated computational approach of the Protein Data Bank structure analysis and atomistic molecular dynamics simulations of glycosylated and deglycosylated proteins. Our study reveals that N-glycosylation does not induce significant changes in protein structure, but decreases protein dynamics, likely leading to an increase in protein stability. Overall, these results suggest not only a common role of glycosylation in proteins, but also a need for certain proteins to be properly glycosylated to gain their intrinsic dynamic properties. | en_US |
dc.description.sponsorship | This work was supported by NIH U54GM087519 and XSEDE MCB070009. We gratefully acknowledge Sunhwan Jo for helping us to use Glycan Reader. Anton computer time was provided by the National Center for Multiscale Modeling of Biological Systems (MMBioS) through Grant P41GM103712-S1 from the National Institutes of Health and the Pittsburgh Supercomputing Center (PSC). The Anton machine at PSC was generously made available by D.E. Shaw Research. | en_US |
dc.publisher | Mcmillan Publishers | en_US |
dc.rights | Copyright © 2015, Macmillan Publishers Limited. All rights reserved This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.title | Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study | en_US |
dc.type | Article | |
kusw.kuauthor | Lee, Hui Sun | |
kusw.kuauthor | Qi, Yifei | |
kusw.kuauthor | Im, Wonpil | |
kusw.kudepartment | Department of Molecular Biosciences | en_US |
dc.identifier.doi | 10.1038/srep08926 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |
Files in this item
This item appears in the following Collection(s)
Except where otherwise noted, this item's license is described as: Copyright © 2015, Macmillan Publishers Limited. All rights reserved
This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/