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Title: Molecular modeling of localized collective motions and dynamics in proteins
Keywords: Protein dynamics, Normal mode, Hydrogen bond, Harmonic approximation,Modified self-consistent approach,Collective motion
Issue Date: 3-Oct-2003
Citation: CAO ZHIWEI (2003-10-03). Molecular modeling of localized collective motions and dynamics in proteins. ScholarBank@NUS Repository.
Abstract: Intramolecular motions in proteins have important functional implications. Examples of functionally important motions are domain motions, localized collective motions, and fluctuational hydrogen bond disruption. In the first part of this thesis, normal mode analysis is used for molecular modeling of collective motions. A possible correlation is identified between normal modes at frequency range of 20~200cm-1 and functionally important torsional motion localized in the flexible linker regions, which is consistent with indications from other studies. In the second part, dynamics of H-bond breaking is modeled by the modified self-consistent harmonic approach (MSHA). The computed hydrogen bond breaking probabilities are found to be consistent with experimental results. Our study suggests the usefulness of harmonic approaches in facilitating the study of functionally important protein motions.
Appears in Collections:Ph.D Theses (Open)

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