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Structure–Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System **
Author(s) -
De Zitter Elke,
Hugelier Siewert,
Duwé Sam,
Vandenberg Wim,
Tebo Alison G.,
Van Meervelt Luc,
Dedecker Peter
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202015201
Subject(s) - spectroscopy , fluorescence , fluorescence spectroscopy , biological system , principal component analysis , function (biology) , molecule , chemical physics , hydrogen bond , molecular machine , photochromism , biophysics , chemistry , materials science , nanotechnology , computer science , biology , physics , evolutionary biology , optics , artificial intelligence , organic chemistry , quantum mechanics
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.