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http://hdl.handle.net/1942/33890
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DC Field | Value | Language |
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dc.contributor.author | De Zitter, Elke | - |
dc.contributor.author | Hugelier, Siewert | - |
dc.contributor.author | DUWE, Sam | - |
dc.contributor.author | Vandenberg, Wim | - |
dc.contributor.author | Tebo, Alison G. | - |
dc.contributor.author | Van Meervelt, Luc | - |
dc.contributor.author | Dedecker, Peter | - |
dc.date.accessioned | 2021-04-08T12:26:12Z | - |
dc.date.available | 2021-04-08T12:26:12Z | - |
dc.date.issued | 2021 | - |
dc.date.submitted | 2021-03-30T12:29:38Z | - |
dc.identifier.citation | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 60 (18), p. 10073-10081 | - |
dc.identifier.issn | 1433-7851 | - |
dc.identifier.uri | http://hdl.handle.net/1942/33890 | - |
dc.description.abstract | Anisotropic environments can drastically alter the spectroscopy and photochemistry of molecules, leading to complex structure-function relationships. We examined this using fluorescent proteins as easy-to-modify model systems. Starting from a single scaffold, we have developed a range of 27 photochromic fluorescent proteins that cover a broad range of spectroscopic properties, including the determination of 43 crystal structures. Correlation and principal component analysis confirmed the complex relationship between structure and spectroscopy, but also allowed us to identify consistent trends and to relate these to the spatial organization. We find that changes in spectroscopic properties can come about through multiple underlying mechanisms, of which polarity, hydrogen bonding and presence of water molecules are key modulators. We anticipate that our findings and rich structure/spectroscopy dataset can open opportunities for the development and evaluation of new and existing protein engineering methods. | - |
dc.description.sponsorship | We are grateful to Gerrit Groenhof (University of Jyvaskyla), Jeremy Harvey (KU Leuven), Raffaele Vitale (Universite de Lille), and Dominique Bourgeois (Institut de Biologie Structurale) for critical insights and discussion. E.D.Z. and L.V.M. thank the beamline staff from X06DA at the Swiss Light Source (Villigen, Switzerland), Proxima1 and Proxima2A at synchrotron Soleil (Gif-sur-Yvette, France), XRD1 at Elettra (Trieste, Italy) and I03 at Diamond Light Source (Oxfordshire, UK) for assistance during X-ray diffraction data collection. E.D.Z., S.H., and S.D. thank the Research Foundation Flanders (FWO) for a doctoral fellowship and postdoctoral fellowships (12X7919N and 12R2817N). This work was supported through funding from the Research Foundation Flanders through grants 1514319 N, G090819N, G0B8817N, and the European Research Council through grant 714688 NanoCellActivity. | - |
dc.language.iso | en | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.subject.other | biophysics | - |
dc.subject.other | fluorescent proteins | - |
dc.subject.other | photochromism | - |
dc.subject.other | structure– | - |
dc.subject.other | function relationships | - |
dc.title | Structure–Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System | - |
dc.type | Journal Contribution | - |
dc.identifier.epage | 10081 | - |
dc.identifier.issue | 18 | - |
dc.identifier.spage | 10073 | - |
dc.identifier.volume | 60 | - |
local.format.pages | 10 | - |
local.bibliographicCitation.jcat | A1 | - |
dc.description.notes | Dedecker, P (corresponding author), Katholieke Univ Leuven, Dept Chem, Celestijnenlaan 200G Box 2403, B-3001 Leuven, Belgium. | - |
dc.description.notes | peter.dedecker@kuleuven.be | - |
dc.description.other | Dedecker, P (corresponding author), Katholieke Univ Leuven, Dept Chem, Celestijnenlaan 200G Box 2403, B-3001 Leuven, Belgium. peter.dedecker@kuleuven.be | - |
local.publisher.place | POSTFACH 101161, 69451 WEINHEIM, GERMANY | - |
local.type.refereed | Refereed | - |
local.type.specified | Article | - |
dc.identifier.doi | 10.1002/anie.202015201 | - |
dc.identifier.pmid | 33543524 | - |
dc.identifier.isi | WOS:000630148800001 | - |
dc.contributor.orcid | Tebo, Alison/0000-0003-0788-5617; Duwe, Sam/0000-0003-3768-1877; Van | - |
dc.contributor.orcid | Meervelt, Luc/0000-0003-2186-5209; Vandenberg, Wim/0000-0002-5888-9100; | - |
dc.contributor.orcid | /0000-0002-6224-652X; Dedecker, Peter/0000-0002-1882-2075 | - |
dc.identifier.eissn | 1521-3773 | - |
local.provider.type | wosris | - |
local.uhasselt.uhpub | yes | - |
local.description.affiliation | [De Zitter, Elke; Hugelier, Siewert; Duwe, Sam; Vandenberg, Wim; Van Meervelt, Luc; Dedecker, Peter] Katholieke Univ Leuven, Dept Chem, Celestijnenlaan 200G Box 2403, B-3001 Leuven, Belgium. | - |
local.description.affiliation | [Tebo, Alison G.] Janelia Res Campus, Howard Hughes Med Inst, 19700 Helix Dr, Ashburn, VA 20147 USA. | - |
local.description.affiliation | [De Zitter, Elke] Univ Grenoble Alpes, CEA, CNRS, IBS, 71 Ave Martyrs, F-38000 Grenoble, France. | - |
local.description.affiliation | [Duwe, Sam] Hasselt Univ, Adv Opt Microscopy Ctr, Agoralaan Bldg C, B-3590 Diepenbeek, Belgium. | - |
local.uhasselt.international | yes | - |
item.fullcitation | De Zitter, Elke; Hugelier, Siewert; DUWE, Sam; Vandenberg, Wim; Tebo, Alison G.; Van Meervelt, Luc & Dedecker, Peter (2021) Structure–Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System. In: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 60 (18), p. 10073-10081. | - |
item.validation | ecoom 2022 | - |
item.accessRights | Open Access | - |
item.fulltext | With Fulltext | - |
item.contributor | De Zitter, Elke | - |
item.contributor | Hugelier, Siewert | - |
item.contributor | DUWE, Sam | - |
item.contributor | Vandenberg, Wim | - |
item.contributor | Tebo, Alison G. | - |
item.contributor | Van Meervelt, Luc | - |
item.contributor | Dedecker, Peter | - |
crisitem.journal.issn | 1433-7851 | - |
crisitem.journal.eissn | 1521-3773 | - |
Appears in Collections: | Research publications |
Files in This Item:
File | Description | Size | Format | |
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rsGreenMutants.pdf | Peer-reviewed author version | 9.01 MB | Adobe PDF | View/Open |
Angew Chem Int Ed - 2021 - De Zitter - Structure Function Dataset Reveals Environment Effects within a Fluorescent Protein.pdf Restricted Access | Published version | 3 MB | Adobe PDF | View/Open Request a copy |
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