Tobacco Mosaic Virus Disassembly By High Hydrostatic Pressure In Combination With Urea And Low Temperature.

dc.creatorBonafe, C F
dc.creatorVital, C M
dc.creatorTelles, R C
dc.creatorGonçalves, M C
dc.creatorMatsuura, M S
dc.creatorPessine, F B
dc.creatorFreitas, D R
dc.creatorVega, J
dc.date1998-Aug
dc.date2015-11-27T12:19:17Z
dc.date2015-11-27T12:19:17Z
dc.date.accessioned2018-03-29T00:52:53Z
dc.date.available2018-03-29T00:52:53Z
dc.identifierBiochemistry. v. 37, n. 31, p. 11097-105, 1998-Aug.
dc.identifier0006-2960
dc.identifier10.1021/bi980349n
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9693006
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194203
dc.identifier9693006
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294436
dc.descriptionWe investigated the effect of low temperature and urea combined with high pressure on tobacco mosaic virus (TMV). The evaluation of its aggregation state and denaturation process was studied using gel filtration, transmission electron microscopy, and spectroscopic methods. The incubation at 2.5 kbar induced 18% dissociation, and decreasing of temperature to -19 degreesC promoted additional dissociation to 72%, with stabilization of the dissociation products. Under such conditions, extensive denaturation did not occur. The apparent enthalpy and entropy of dissociation (Delta and TDelta) were -9.04 kcal/mol subunit and -15.1 kcal/mol subunit, respectively, indicating that the TMV association is an entropicly driven process. The apparent free energy of stabilization given by the presence of RNA is at least -1.7 kcal/mol subunit. Urea-induced dissociation of TMV samples and incubation at high-pressure promoted a higher degree of dissociation. The volume change of dissociation decreased in magnitude from -16.3 to -3.1 mL/mol of dissociated subunit, respectively, in the absence and presence of 2.5 M urea, suggesting exposure of the protein-protein interface to the solvent. High-pressure induced remarkable TMV denaturation in the presence of 2.5 M urea, with a volume change of -101 mL/mol of denatured subunit. The apparent enthalpy and entropy of denaturation (Delta and TDelta) by 1.75 M urea at 2.5 kbar was -11.1 and -10.2 kcal/mol subunit, respectively, demonstrating that the TMV protein coat presents an apparent free energy of denaturation by urea close to zero. Although the processes could not be assumed to be pure equilibria, these thermodynamic parameters could be derived by assuming a steady-state condition.
dc.description37
dc.description11097-105
dc.languageeng
dc.relationBiochemistry
dc.relationBiochemistry
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAtmospheric Pressure
dc.subjectCold Temperature
dc.subjectHydrostatic Pressure
dc.subjectKinetics
dc.subjectLight
dc.subjectMicroscopy, Electron
dc.subjectProtein Denaturation
dc.subjectScattering, Radiation
dc.subjectSpectrometry, Fluorescence
dc.subjectTobacco Mosaic Virus
dc.subjectUrea
dc.subjectViral Proteins
dc.subjectVirus Assembly
dc.titleTobacco Mosaic Virus Disassembly By High Hydrostatic Pressure In Combination With Urea And Low Temperature.
dc.typeArtículos de revistas


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