Dynamics of water in biological recognition.

  title={Dynamics of water in biological recognition.},
  author={Samir Kumar Pal and Ahmed H. Zewail},
  journal={Chemical reviews},
  volume={104 4},
Almost all biological macromoleculess proteins (enzymes) and DNAs are inactive in the absence of water. Hydration of a protein/enzyme is particularly important for the stability of the structure and for the function, especially the recognition at a specific site. This role of hydration in enzyme catalysis is well known and has recently been reviewed in a number of publications. In one of these studies it was shown that the dehydration of a protein, which makes it more rigid and… 
Nucleic Acids: Hydration
The need for additional physico-chemical studies of DNA hydration by experimental and theoretic scientists is emphasized and the importance of hydration as a major contributor to the energetics of nucleic acid recognition is highlighted.
Water mediation in protein folding and molecular recognition.
  • Y. LevyJ. Onuchic
  • Biology, Chemistry
    Annual review of biophysics and biomolecular structure
  • 2006
Focusing on water sheds light on the physics and function of biological machinery and self-assembly and may advance the understanding of the natural design of proteins and nucleic acids.
Biomolecular Solvation in Theory and Experiment
The modern understanding of biological macromolecules is unthinkable without a consideration of the solvent environment [1] . Solvent is crucial for the functioning of biological systems both
Site-Resolved Measurement of Water-Protein Interactions by Solution NMR
Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters, and an unprecedented clustering of different hydration-dynamics classes of sites is evident.
Heme proteins: the role of solvent in the dynamics of gates and portals.
A fingerprint of protein solvation state, the hydration sites map, is provided, which may represent a novel tool for comparing different forms/species of globular proteins.
Thermal breaking of spanning water networks in the hydration shell of proteins.
Computer simulations of the clustering and percolation of water in the hydration shell of a small elastinlike peptide and the medium-size protein staphylococcal nuclease, in aqueous solution, have found that in both systems a spanning network of hydration water exists at low temperatures and breaks up with increasing temperature via a quasi-two-dimensional percolations transition.
Protein hydration dynamics in solution: a critical survey.
  • B. Halle
  • Chemistry
    Philosophical transactions of the Royal Society of London. Series B, Biological sciences
  • 2004
The aim here is to critically examine central concepts in the description of protein hydration, and to assess the experimental basis for the current view of protein Hydration, with the focus on dynamic aspects.
Hydration dynamics at fluorinated protein surfaces
Using ultrafast fluorescence spectroscopy, it is found that fluorinated side chains exert electrostatic drag on neighboring water molecules, slowing water motion at the protein surface.
Hydration of proteins and nucleic acids: Advances in experiment and theory. A review.


Protein-solvent interactions
The new paradigm for protein research solvent interactions with proteins as revealed by X-ray crystallographic studies protein hydration and glass transition behavior dielectric studies of protein
The Mechanisms of Fast Reactions in Solution
This text deals with the contribution of fast reaction techniques to our understanding of events on the molecular scale during chemical reactions. It covers the advances resulting from the
Principles of fluorescence spectroscopy
This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.