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dc.contributor.advisor Huang, Huey W.
dc.creatorCao, Hung Duc
dc.date.accessioned 2009-06-04T00:42:47Z
dc.date.available 2009-06-04T00:42:47Z
dc.date.issued 1995
dc.identifier.urihttps://hdl.handle.net/1911/16803
dc.description.abstract The incoherent quasi-elastic neutron scattering (IQNS) method is a useful technique to study biomolecular dynamics. The versatility of the method makes possible motional studies of biomolecules in different forms: powder, crystal, and solution; and at different temperatures. Thus, it allows for the investigation of biomolecular dynamics over a wide-range of physical conditions. We have used the IQNS method to study the motions of side chains in trypsin and myoglobin at various D$\sb2$O hydration levels. The scattering spectra S(Q,$\omega$) were measured in constant-Q mode. The protein in powder form exhibits vibrational high-frequency motions, while the protein in solution and in crystals are characterized by diffusive jumps, and high-frequency vibrations. At temperatures below 200K, the S(Q,$\omega$) for these proteins in solution is similar to an harmonic solid. As temperature increases, a transition is seen at 200K, above which the protein becomes more liquid-like with rapid transitions between conformational substates. The diffusion constant D for the side chains is on the order of 10$\sp{-6}$ cm$\sp2$/sec.
dc.format.extent 88 p.
dc.format.mimetype application/pdf
dc.language.iso eng
dc.subjectBiophysics
Molecular physics
dc.title Protein dynamics at various hydration levels using the incoherent quasielastic neutron scattering technique
dc.type.genre Thesis
dc.type.material Text
thesis.degree.department Biophysics
thesis.degree.discipline Engineering
thesis.degree.grantor Rice University
thesis.degree.level Doctoral
thesis.degree.name Doctor of Philosophy
dc.identifier.citation Cao, Hung Duc. "Protein dynamics at various hydration levels using the incoherent quasielastic neutron scattering technique." (1995) Diss., Rice University. https://hdl.handle.net/1911/16803.


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