Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorTung, Dickson.-
dc.description.abstractIt is a general belief that the electrostatic field arising from the electrostatic polarization of an alpha helix is important in protein folding and its stability. In this experiment, polarized protein-specific charges update are employ to introduce this effect into conventional molecular dynamic simulation. Simulation for 3 alanine-based peptides, Ac-AAQAAAAQAAGY-NH2, Ac-AAKAAAAKAAGY-NH2,and Ac-AADAAAADAAGY-NH2 in 40% trifluoroethanol are done. As a comparison, simulation was also done using conventional force fields. Without proper inclusion of electronic polarization effect, the structure generated from the simulation are fairly similar with each other which suggest the system is unable to distinguish the substitution of amino acid. However, helix content calculated and detailed analysis of data produced from PPC update system matches experimental values thus suggesting that PPC update provides a better representation of electronic density on peptide atoms. Hydrogen bonds on alpha helix backbone are also more stable with the implementation of electronic polarization which is critcal to the stability of secondary structures on protein.en_US
dc.format.extent18 p.en_US
dc.subjectDRNTU::Science::Chemistry::Physical chemistry::Electrochemistryen_US
dc.titleEffect of electronic polarization on alanine-based peptides' alpha helices.en_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.schoolSchool of Physical and Mathematical Sciencesen_US
dc.description.degreeBachelor of Science in Chemistry and Biological Chemistryen_US
dc.contributor.supervisor2Zhang Daweien_US
item.fulltextWith Fulltext-
Appears in Collections:SPMS Student Reports (FYP/IA/PA/PI)
Files in This Item:
File Description SizeFormat 
Tung Dickson.pdf
  Restricted Access
7.56 MBAdobe PDFView/Open

Page view(s)

Updated on Jan 20, 2021


Updated on Jan 20, 2021

Google ScholarTM


Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.