期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 60, 期 18, 页码 10073-10081出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202015201
关键词
biophysics; fluorescent proteins; photochromism; structure– function relationships
资金
- Research Foundation Flanders (FWO) [12X7919N, 12R2817N]
- Research Foundation Flanders [1514319 N, G090819N, G0B8817N]
- European Research Council [714688]
Anisotropic environments can significantly impact the spectroscopy and photochemistry of molecules, leading to complex structure-function relationships. By studying fluorescent proteins as model systems, it was found that changes in spectroscopic properties can be attributed to multiple underlying mechanisms. The research highlights the complex interplay between structure and spectroscopy, identifying key modulators like polarity, hydrogen bonding, and presence of water molecules.
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.
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