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Exploring the dynamics of allostery through multi-dimensional crystallography. | LitMetric

Exploring the dynamics of allostery through multi-dimensional crystallography.

Biophys Rev

Institute for Nanostructure and Solid-State Physics, University of Hamburg, Hamburg, Germany.

Published: October 2024

AI Article Synopsis

  • The review explores the use of multi-dimensional crystallography to understand how time and temperature affect allosteric proteins.
  • * It highlights the relationship between a protein's structure, its dynamics, and its function.
  • * The study emphasizes that advancing structural biology techniques can help reveal important details about the molecular processes essential for life.*

Article Abstract

By delving into the applications, methodologies, and case studies of multi-dimensional crystallography, whereby time and temperature are varied in the context of allostery, this review aims to elucidate the intricate interplay between structure, dynamics, and function in allosteric proteins. As the field of structural biology continues to advance, integrating multi-dimensional approaches promises to unlock new frontiers in our quest to decipher the molecular mechanisms governing life.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11604904PMC
http://dx.doi.org/10.1007/s12551-024-01224-3DOI Listing

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