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Atomistic Simulations for Investigating Structural Stability and Selecting Initial Adsorption Orientation of Lysozyme and Apo-α-Lactalbumin at Hydrophobic and Hydrophilic Surfaces
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- Author / Creator
- Pansri, Siriporn
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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. -
- Subjects / Keywords
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- Graduation date
- Fall 2012
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- Type of Item
- Thesis
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- Degree
- Master of Science
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- License
- This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.