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Deducing fast electron density changes in randomly orientated uncrystallized biomolecules in a pump-probe experiment.

K Pande1, P Schwander1, M Schmidt1

  • 1Department of Physics, University of Wisconsin-Milwaukee, Milwaukee, WI 53211, USA.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|June 11, 2014
PubMed
Summary

We developed a new method to observe structural changes in biomolecules in solution using X-ray scattering. This technique allows direct calculation of electron density differences, revealing molecular dynamics.

Keywords:
X-ray free-electron laserproteinstime-resolved

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Studying dynamic structural changes in uncrystallized biomolecules in solution is challenging.
  • Traditional methods often require crystallization, which can alter native structures.
  • Time-resolved techniques are crucial for understanding biomolecular function.

Purpose of the Study:

  • To develop a novel method for time-resolved structural analysis of biomolecules in solution.
  • To enable direct calculation of difference electron density for photoexcited states.
  • To provide insights into the dynamics of uncrystallized biological molecules.

Main Methods:

  • Measuring angular correlations of intensities from numerous diffraction patterns of randomly oriented biomolecules.
  • Employing a pump-probe experimental setup analogous to small-angle X-ray scattering.
  • Utilizing a derived linear relationship between correlation function differences and difference electron density.

Main Results:

  • Successfully deduced time-resolved structural changes in uncrystallized biomolecules.
  • Enabled direct calculation of difference electron density by comparing photoexcited and dark states.
  • Demonstrated the applicability of the method for small structural changes.

Conclusions:

  • The proposed method offers a powerful approach for studying dynamic structural changes in solution.
  • It bypasses the need for crystallization, preserving the native state of biomolecules.
  • Provides a direct route to visualizing structural alterations upon photoexcitation.