{ "dc.contributor.author": "Font Sentias, Josep" , "dc.contributor.author": "Torrent i Mas, Joan" , "dc.contributor.author": "Ribó i Panosa, Marc" , "dc.contributor.author": "Laurents, Douglas V." , "dc.contributor.author": "Balny, Claude" , "dc.contributor.author": "Vilanova i Brugués, Maria" , "dc.contributor.author": "Lange, Reinhard" , "dc.date.accessioned": "2011-09-15T08:11:08Z" , "dc.date.available": "2011-09-15T08:11:08Z" , "dc.date.issued": "2006" , "dc.identifier.citation": "Font, J., Torrent, J., Ribo, M., Laurents, D.V., Balny, C., Vilanova, M., et al. (2006). Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A. Biophysical Journal, 91 (6), 2264-2274. Recuperat 15 setembre de 2011, a doi:10.1529/biophysj.106.082552" , "dc.identifier.issn": "0006-3495" , "dc.identifier.uri": "http://hdl.handle.net/10256/3564" , "dc.description.abstract": "Pressure-jump (p-jump)-induced relaxation kinetics was used to explore the energy landscape of protein folding/unfolding of Y115W, a fluorescent variant of ribonuclease A. Pressure-jumps of 40MPa amplitude (5ms dead-time) were conducted both to higher (unfolding) and to lower (folding) pressure, in the range from 100 to 500MPa, between 30 and 50°C. Significant deviations from the expected symmetrical protein relaxation kinetics were observed. Whereas downward p-jumps resulted always in single exponential kinetics, the kinetics induced by upward p-jumps were biphasic in the low pressure range and monophasic at higher pressures. The relative amplitude of the slow phase decreased as a function of both pressure and temperature. At 50°C, only the fast phase remained. These results can be interpreted within the framework of a two-dimensional energy surface containing a pressure- and temperature-dependent barrier between two unfolded states differing in the isomeric state of the Asn-113–Pro-114 bond. Analysis of the activation volume of the fast kinetic phase revealed a temperature-dependent shift of the unfolding transition state to a larger volume. The observed compensation of this effect by glycerol offers an explanation for its protein stabilizing effect" , "dc.format.mimetype": "application/pdf" , "dc.language.iso": "eng" , "dc.publisher": "Biophysical Society" , "dc.relation.isformatof": "Reproducció digital del document publicat a: http://dx.doi.org/10.1529/biophysj.106.082552" , "dc.relation.ispartof": "© Biophysical Journal, 2006, vol.91, núm.6, p.2264-2274" , "dc.relation.ispartofseries": "Articles publicats (D-B)" , "dc.rights": "Tots els drets reservats" , "dc.subject": "Cinemàtica" , "dc.subject": "Glicerina" , "dc.subject": "Ribonucleases" , "dc.subject": "Glycerol" , "dc.subject": "Kinematics" , "dc.title": "Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A" , "dc.type": "info:eu-repo/semantics/article" , "dc.rights.accessRights": "info:eu-repo/semantics/openAccess" , "dc.type.version": "info:eu-repo/semantics/publishedVersion" , "dc.identifier.doi": "http://dx.doi.org/10.1529/biophysj.106.082552" , "dc.identifier.idgrec": "004509" }