Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films
Thesis (M.Sc.)--Memorial University of Newfoundland, 2009. Physics Includes bibliographical references (leaves 99-108) Molecular dynamics simulations of the fragment Mini-B of Surfactant Protein B were carried out in the NVT ensemble for simulation times ranging from 20 ns to 80 ns. These simulation...
Main Author: | |
---|---|
Other Authors: | |
Format: | Thesis |
Language: | English |
Published: |
2009
|
Subjects: | |
Online Access: | http://collections.mun.ca/cdm/ref/collection/theses4/id/69452 |
id |
ftmemorialunivdc:oai:collections.mun.ca:theses4/69452 |
---|---|
record_format |
openpolar |
spelling |
ftmemorialunivdc:oai:collections.mun.ca:theses4/69452 2023-05-15T17:23:33+02:00 Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films Gupta, Santosh K. (Santosh Kumar), 1982- Memorial University of Newfoundland. Dept. of Physics 2009 x, 108 leaves : ill. (chiefly col.) Image/jpeg; Application/pdf http://collections.mun.ca/cdm/ref/collection/theses4/id/69452 Eng eng Electronic Theses and Dissertations (10.14 MB) -- http://collections.mun.ca/PDFs/theses/Gupta_SantoshK.pdf a3242490 http://collections.mun.ca/cdm/ref/collection/theses4/id/69452 The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission. Paper copy kept in the Centre for Newfoundland Studies, Memorial University Libraries Lipoproteins Monomolecular films Pulmonary surfactant Surface tension Text Electronic thesis or dissertation 2009 ftmemorialunivdc 2015-08-06T19:22:05Z Thesis (M.Sc.)--Memorial University of Newfoundland, 2009. Physics Includes bibliographical references (leaves 99-108) Molecular dynamics simulations of the fragment Mini-B of Surfactant Protein B were carried out in the NVT ensemble for simulation times ranging from 20 ns to 80 ns. These simulations were performed in DPPC:POPG monolayers and POPG monolayers at different cross-sectional areas per lipid, varying the initial depth and orientation of the peptide. Analysis was carried out to determine what depth the peptide can attain in the monolayers towards the end of the simulations. Secondary structure of the peptide was also examined, and it was found that in the majority of cases both alpha helices remained alpha helical to a reasonable degree in the monolayers. The tilt angles of the alpha helices of Mini-B in the DPPC:POPG monolayers seemed to show relatively small deviations from those of the corresponding structure determined in SDS micelles by NMR, provided that the peptide was placed at a low enough depth. A study was also performed to determine the effect of sodium ions on the interaction between the cationic Arginine and Lysine residues of Mini-B and the anionic phosphate headgroups of POPG. Thesis Newfoundland studies University of Newfoundland Memorial University of Newfoundland: Digital Archives Initiative (DAI) |
institution |
Open Polar |
collection |
Memorial University of Newfoundland: Digital Archives Initiative (DAI) |
op_collection_id |
ftmemorialunivdc |
language |
English |
topic |
Lipoproteins Monomolecular films Pulmonary surfactant Surface tension |
spellingShingle |
Lipoproteins Monomolecular films Pulmonary surfactant Surface tension Gupta, Santosh K. (Santosh Kumar), 1982- Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
topic_facet |
Lipoproteins Monomolecular films Pulmonary surfactant Surface tension |
description |
Thesis (M.Sc.)--Memorial University of Newfoundland, 2009. Physics Includes bibliographical references (leaves 99-108) Molecular dynamics simulations of the fragment Mini-B of Surfactant Protein B were carried out in the NVT ensemble for simulation times ranging from 20 ns to 80 ns. These simulations were performed in DPPC:POPG monolayers and POPG monolayers at different cross-sectional areas per lipid, varying the initial depth and orientation of the peptide. Analysis was carried out to determine what depth the peptide can attain in the monolayers towards the end of the simulations. Secondary structure of the peptide was also examined, and it was found that in the majority of cases both alpha helices remained alpha helical to a reasonable degree in the monolayers. The tilt angles of the alpha helices of Mini-B in the DPPC:POPG monolayers seemed to show relatively small deviations from those of the corresponding structure determined in SDS micelles by NMR, provided that the peptide was placed at a low enough depth. A study was also performed to determine the effect of sodium ions on the interaction between the cationic Arginine and Lysine residues of Mini-B and the anionic phosphate headgroups of POPG. |
author2 |
Memorial University of Newfoundland. Dept. of Physics |
format |
Thesis |
author |
Gupta, Santosh K. (Santosh Kumar), 1982- |
author_facet |
Gupta, Santosh K. (Santosh Kumar), 1982- |
author_sort |
Gupta, Santosh K. (Santosh Kumar), 1982- |
title |
Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
title_short |
Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
title_full |
Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
title_fullStr |
Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
title_full_unstemmed |
Molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
title_sort |
molecular dynamics of a respiratory protein fragment in phospholipid monomolecular films |
publishDate |
2009 |
url |
http://collections.mun.ca/cdm/ref/collection/theses4/id/69452 |
genre |
Newfoundland studies University of Newfoundland |
genre_facet |
Newfoundland studies University of Newfoundland |
op_source |
Paper copy kept in the Centre for Newfoundland Studies, Memorial University Libraries |
op_relation |
Electronic Theses and Dissertations (10.14 MB) -- http://collections.mun.ca/PDFs/theses/Gupta_SantoshK.pdf a3242490 http://collections.mun.ca/cdm/ref/collection/theses4/id/69452 |
op_rights |
The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission. |
_version_ |
1766113262058864640 |