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dc.contributor.authorTehei, Moeava
dc.contributor.authorSmith, Jeremy C.
dc.contributor.authorMonk, Colin R.
dc.contributor.authorOllivier, Jacques
dc.contributor.authorOettl, Martin
dc.contributor.authorKurkal, Vandana
dc.contributor.authorFinney, John L.
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2008-11-07T00:17:34Z
dc.date.available2008-11-07T00:17:34Z
dc.date.issued2006-10
dc.identifier.citationTehei, M., Smith, J.C., Monk, C., Ollivier, J., Oettl, M., Kurkal, V., Finney, J. L. & Daniel, R.M. (2006). Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering. Biophysical Journal, 90, 1090- 1097.en_US
dc.identifier.issn1542-0086
dc.identifier.urihttps://hdl.handle.net/10289/1288
dc.description.abstractThe internal dynamics of native and immobilized Escherichia coli dihydrofolate reductase (DHFR) have been examined using incoherent quasielastic neutron scattering. These results reveal no difference between the high frequency vibration mean-square displacement of the native and the immobilized E. coli DHFR. However, length-scale-dependent, picosecond dynamical changes are found. On longer length scales, the dynamics are comparable for both DHFR samples. On shorter length scales, the dynamics is dominated by local jump motions over potential barriers. The residence time for the protons to stay in a potential well is = 7.95 ± 1.02 ps for the native DHFR and = 20.36 ± 1.80 ps for the immobilized DHFR. The average height of the potential barrier to the local motions is increased in the immobilized DHFR, and may increase the activation energy for the activity reaction, decreasing the rate as observed experimentally. These results suggest that the local motions on the picosecond timescale may act as a lubricant for those associated with DHFR activity occurring on a slower millisecond timescale. Experiments indicate a significantly slower catalytic reaction rate for the immobilized E. coli DHFR. However, the immobilization of the DHFR is on the exterior of the enzyme and essentially distal to the active site, thus this phenomenon has broad implications for the action of drugs distal to the active site.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherBiophysical Societyen_NZ
dc.relation.urihttp://www.biophysj.org/cgi/content/abstract/90/3/1090en_US
dc.rightsThis article has been published in the journal: Biophysical Journal. Copyright © 2006 by the Biophysical Society.en_US
dc.titleDynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scatteringen_US
dc.typeJournal Articleen_US
dc.identifier.doi10.1529/biophysj.105.062182en_NZ
dc.relation.isPartOfBiophysical Journalen_NZ
pubs.begin-page1090en_NZ
pubs.elements-id32145
pubs.end-page1097en_NZ
pubs.issue3en_NZ
pubs.volume90en_NZ


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