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Structure‐function dataset reveals environment effects within a fluorescent protein model system

DOI: 10.1002/anie.202015201 DOI Help

Authors: Elke De Zitter (KU Leuven) , Siewert Hugelier (KU Leuven) , Sam Duwé (KU Leuven) , Wim Vandenberg (KU Leuven) , Alison G. Tebo (Howard Hughes Medical Institute) , Luc Van Meervelt (KU Leuven) , Peter Dedecker (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition

State: Published (Approved)
Published: February 2021

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.

Journal Keywords: Structure-Function Relationships; Photochromism; biophysics; fluorescent proteins

Subject Areas: Chemistry

Instruments: I02-Macromolecular Crystallography

Other Facilities: X06DA at Swiss Light Source; Proxima1 and Proxima2A at Soleil; XRD1 at Elettra

Added On: 17/02/2021 08:23

Discipline Tags:

Biochemistry Technique Development - Chemistry Chemistry Structural biology Organic Chemistry Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)