We are excited to announce that the repository will soon undergo an upgrade, featuring a new look and feel along with several enhanced features to improve your experience. Please be on the lookout for further updates and announcements regarding the launch date. We appreciate your support and look forward to unveiling the improved platform soon.
dc.contributor.author | Gall, Andrew![]() |
|
dc.contributor.author | Ilioaia, Cristian![]() |
|
dc.contributor.author | Kruger, T.P.J. (Tjaart)![]() |
|
dc.contributor.author | Novoderezhkin, Vladimir I.![]() |
|
dc.contributor.author | Robert, Bruno![]() |
|
dc.contributor.author | Van Grondelle, Rienk![]() |
|
dc.date.accessioned | 2015-10-30T07:34:30Z | |
dc.date.available | 2015-10-30T07:34:30Z | |
dc.date.issued | 2015-06 | |
dc.description.abstract | Among the ultimate goals of protein physics, the complete, experimental description of the energy paths leading to protein conformational changes remains a challenge. Single protein fluorescence spectroscopy constitutes an approach of choice for addressing protein dynamics, and, among naturally fluorescing proteins, light-harvesting (LH) proteins from purple bacteria constitute an ideal object for such a study. LHs bind bacteriochlorophyll a molecules, which confer on them a high intrinsic fluorescence yield. Moreover, the electronic properties of these pigment-proteins result from the strong excitonic coupling between their bound bacteriochlorophyll a molecules in combination with the large energetic disorder due to slow fluctuations in their structure. As a result, the position and probability of their fluorescence transition delicately depends on the precise realization of the disorder of the set of bound pigments, which is governed by the LH protein dynamics. Analysis of these parameters using time-resolved single-molecule fluorescence spectroscopy thus yields direct access to the protein dynamics. Applying this technique to the LH2 protein from Rhodovulum (Rdv.) sulfidophilum, the structure—and consequently the fluorescence properties—of which depends on pH, allowed us to follow a single protein, pH-induced, reversible, conformational transition. Hence, for the first time, to our knowledge, a protein transition can be visualized through changes in the electronic structure of the intrinsic cofactors, at a level of a single LH protein, which opens a new, to our knowledge, route for understanding the changes in energy landscape that underlie protein function and adaptation to the needs of living organisms. | en_ZA |
dc.description.librarian | hb2015 | en_ZA |
dc.description.sponsorship | The French Infrastructure for Integrated Structural Biology (FRISBI) ANR-10-INSB-05-01 (A.G., C.I., B.R); the European Research Council (ERC) through an Advanced Investigator Grant, contract No. 267333 (R.v.G., B.R.); the French Agence Nationale de la Recherche´ (ANR) through a Chaire d’excellence, ANR-07-CEX- 009-01 (A.G.); The Ile-de-France Region (France) through a Blaise Pascal International Research Chair (R.v.G.); the European Union (EU) FP6 Marie Curie Early Stage Training Network via the Advanced Training in Laser Sciences project (T.P.J.K.); the EU FP7 Marie Curie Reintegration Grant No. ERG 224796 (C.I.); the EU LASERLAB-EUROPE (A.G., grant agreement No. 284464, 7th Framework Programme) and Access to Research Infrastructures action of the Improving Human Potential Program, contract No. RII-CT-2003-506350 (A.G.); the van Gogh programme of the Earth and Life Sciences council of the Netherlands Foundation for Scientific Research (NWO-ALW) and the French Ministry for Foreign and European Affairs (MAEE), contract No. 25024VJ (A.G., C.I., B.R., R.v.G.); CEA-Eurotalents program, European Union contract no. PCOFUND-GA-2008-228664 (C.I.); TOP grant (700.58.305) from the Foundation of Chemical Sciences, part of the Netherlands Organization for Scientific Research (C.I. and R.v.G.). R.v.G. gratefully acknowledges his Academy Professor grant from the Royal Netherlands Academy of Arts and Sciences (KNAW). | en_ZA |
dc.description.uri | http://www.cell.combiophysj | en_ZA |
dc.identifier.citation | Gall, A, Ilioaia, C, Krüger, TPJ, Novoderezhkin, VI, Robert, B & Van Grondelle, R 2015, 'Conformational switching in a light-harvesting protein as followed by single-molecule spectroscopy', Biophysical Journal, vol. 108, no. 11, pp. 2713-2720. | en_ZA |
dc.identifier.issn | 0006-3495 (print) | |
dc.identifier.issn | 1542-0086 (online) | |
dc.identifier.other | 10.1016/j.bpj.2015.04.017 | |
dc.identifier.uri | http://hdl.handle.net/2263/50277 | |
dc.language.iso | en | en_ZA |
dc.publisher | Biophysical Society | en_ZA |
dc.rights | © 2015 The Authors.This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). | en_ZA |
dc.subject | Conformational switching | en_ZA |
dc.subject | Light-harvesting protein | en_ZA |
dc.subject | Single-molecule spectroscopy | en_ZA |
dc.title | Conformational switching in a light-harvesting protein as followed by single-molecule spectroscopy | en_ZA |
dc.type | Article | en_ZA |