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Area of Science:

  • Life Sciences
  • Biophysics
  • Biochemistry

Background:

  • Fluorescent protein-based biosensors are vital in life sciences, offering biocompatibility and tunable emission.
  • Current development relies heavily on trial and error, hindering rational design.
  • Understanding the working mechanisms of calcium (Ca2+) biosensors is crucial for their optimization.

Purpose of the Study:

  • To elucidate the working mechanisms of a Pro377Arg mutant Ca2+ biosensor.
  • To investigate the excited-state proton-transfer (ESPT) reaction dynamics.
  • To provide design principles for enhancing biosensor efficiency and photostability.

Main Methods:

  • Tunable femtosecond stimulated Raman spectroscopy (FSRS).
  • Transient absorption spectroscopy.
  • Quantum chemical calculations.
  • Comparative analysis of Ca2+-free/bound states and parent protein.

Main Results:

  • The Ca2+-bound biosensor exhibits faster ESPT and increased structural inhomogeneity compared to the parent protein.
  • Correlated vibrational modes reveal enhanced chromophore twisting and trapping in the Ca2+-bound state during ESPT.
  • Chromophore dynamics remain largely conserved in the Ca2+-free state.

Conclusions:

  • Structural dynamics insights into the ESPT reaction are uncovered.
  • Design principles for improved Ca2+ biosensors include maintaining a hydrophilic, less compact, and homogeneous environment with directional H-bonding.
  • Bioengineering strategies can enhance ESPT efficiency and quantum yield while preserving photostability.