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Fast internal dynamics in alcohol dehydrogenase.

M Monkenbusch1, A Stadler1, R Biehl1

  • 1Jülich Centre for Neutron Science JCNS and Institute for Complex Systems ICS, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany.

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|August 24, 2015
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Summary

High-resolution neutron spectroscopy revealed fast internal motions in alcohol dehydrogenase (ADH). About one-third of ADH protons exhibit localized diffusion, suggesting movement in solvent-exposed residues.

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Area of Science:

  • Biophysics
  • Protein dynamics
  • Neutron spectroscopy

Background:

  • Large-scale domain motions in alcohol dehydrogenase (ADH) were previously observed using neutron spin-echo spectroscopy (NSE).
  • Understanding protein dynamics is crucial for enzyme function and stability.

Purpose of the Study:

  • To investigate the dynamics of alcohol dehydrogenase (ADH) in solution using high-resolution neutron spectroscopy.
  • To identify and characterize internal motions beyond the slow domain movements.

Main Methods:

  • Utilized high-resolution neutron time-of-flight (TOF) and neutron backscattering (BS) spectroscopy.
  • Analyzed hydrogen dynamics in the incoherent scattering range.
  • Interpreted data using three distinct mobility classes.

Main Results:

  • Identified a fast internal dynamic process in ADH, in addition to slow global diffusion and domain motions.
  • Approximately one-third of ADH protons participate in this fast, localized diffusive motion.
  • The diffusion coefficient for these internal motions is about two-thirds that of the surrounding D2O solvent.

Conclusions:

  • The fast internal process is likely associated with solvent-exposed amino acid residues, particularly those with dangling side chains.
  • This study provides new insights into the complex dynamic behavior of ADH at a finer resolution.