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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Hydration of cement is a chemical reaction between cement particles and water. This process occurs primarily through two mechanisms: through-solution and topochemical. In the through-solution process, anhydrous compounds dissolve into their constituents, hydrates form in the solution, and then precipitate from the supersaturated solution. The topochemical process involves solid-state reactions at the cement particle surface. The through-solution process dominates the topochemical process at the...
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Hydration Water Distribution around Intrinsically Disordered Proteins.

Leena Aggarwal1, Parbati Biswas1

  • 1Department of Chemistry , University of Delhi , Delhi 110007 , India.

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Summary

Intrinsically disordered proteins exhibit higher hydration water density and order compared to globular proteins due to their unique structures. This study provides the first theoretical analysis of 3D hydration water distribution around disordered proteins.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) lack stable tertiary structures, influencing their interactions with water.
  • Understanding hydration water is crucial for elucidating IDP function and dynamics.

Purpose of the Study:

  • To investigate the distribution and local structural order of hydration water around IDPs.
  • To compare hydration properties of IDPs with those of globular proteins using theoretical methods.

Main Methods:

  • Employed three-dimensional (3D)-reference interaction site model (3D-RRISM) theory.
  • Quantified water distribution using 3D distribution functions and water-protein radial distribution functions (RDFs).
  • Assessed local water ordering via the tetrahedral order parameter.

Main Results:

  • IDPs show higher hydration water density than globular proteins due to noncompact structures and increased solvent-accessible surface area.
  • Residue-specific RDFs reveal distinct water-protein interactions for charged and hydrophobic residues in IDPs versus globular proteins.
  • Water molecules exhibit greater local ordering around IDPs, correlated with higher mean net charge and stronger water-protein interactions.

Conclusions:

  • Disordered proteins possess unique hydration shells characterized by higher water density and order.
  • These findings highlight the significant role of hydration in the behavior and function of intrinsically disordered proteins.