ERA

Download the full-sized PDF of Atomistic Simulations for Investigating Structural Stability and Selecting Initial Adsorption Orientation of Lysozyme and Apo-α-Lactalbumin at Hydrophobic and Hydrophilic SurfacesDownload the full-sized PDF

Analytics

Share

Permanent link (DOI): https://doi.org/10.7939/R36403

Download

Export to: EndNote  |  Zotero  |  Mendeley

Communities

This file is in the following communities:

Graduate Studies and Research, Faculty of

Collections

This file is in the following collections:

Theses and Dissertations

Atomistic Simulations for Investigating Structural Stability and Selecting Initial Adsorption Orientation of Lysozyme and Apo-α-Lactalbumin at Hydrophobic and Hydrophilic Surfaces Open Access

Descriptions

Other title
Subject/Keyword
adsorption orientation
Apo-α-Lactalbumin
lysozyme
protein adsorption
stability
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Pansri, Siriporn
Supervisor and department
Unsworth, Larry (Chemical and Materials Engineering)/Kovalenko, Andriy (Mechanical Engineering)
Examining committee member and department
Yeung, Anthony (Chemical and Materials Engineering)
Kovalenko, Andriy (Mechanical Engineering)
Unsworth, Larry (Chemical and Materials Engineering)
Department
Department of Chemical and Materials Engineering
Specialization
Materials Engineering
Date accepted
2012-08-22T13:49:00Z
Graduation date
2012-11
Degree
Master of Science
Degree level
Master's
Abstract
Molecular dynamics (MD) simulations were performed to investigate the structural stability of lysozyme and apo-α-lactalbumin under physiological pH and solution. Upon introduction to the solution, apo-α-lactalbumin showed lower stability than lysozyme with higher backbone root mean square fluctuation (RMSF) of the exposed residues and C-terminus, in- cluding secondary structure transition from α-helices to turns in residues 105-110. However, no noticeable changes were observed in the secondary structure of lysozyme during the simulations. Subsequently, molecular mechanics (MM) simulations were carried out to determine the preferred orientation for adsorption of these proteins at poly (ethylene oxide) (PEO) films capped with hydroxyl and methoxy end-groups, based on the Lenard- Jones (L-J) potential. Both proteins preferred to initially adsorb at hy- drophilic surface with its side-on orientation which clef faces sideways. At hydrophobic surface, the preferred orientation of lysozyme became a back- on orientation which clef faces outward, whereas that of apo-α-lactalbumin remained a side-on orientation.
Language
English
DOI
doi:10.7939/R36403
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
Citation for previous publication

File Details

Date Uploaded
Date Modified
2014-04-30T23:34:52.517+00:00
Audit Status
Audits have not yet been run on this file.
Characterization
File format: pdf (Portable Document Format)
Mime type: application/pdf
File size: 5353912
Last modified: 2015:10:12 16:56:59-06:00
Filename: Pansri_Siriporn_Fall 2012.pdf
Original checksum: 8d729d51d61bfa5239fc30c58f218369
Well formed: true
Valid: true
Page count: 112
Activity of users you follow
User Activity Date