Hydration of proteins and nucleic acids: Advances in experiment and theory. A review
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
27241846
DOI
10.1016/j.bbagen.2016.05.036
PII: S0304-4165(16)30180-5
Knihovny.cz E-resources
- Keywords
- Bioinformatics, Biomolecular recognition, Hydration, Molecular biophysics, Molecular modeling and simulation, Structural biology,
- MeSH
- Nucleic Acids metabolism MeSH
- Proteins metabolism MeSH
- Molecular Dynamics Simulation MeSH
- Water metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Nucleic Acids MeSH
- Proteins MeSH
- Water MeSH
BACKGROUND: Most biological processes involve water, and the interactions of biomolecules with water affect their structure, function and dynamics. SCOPE OF REVIEW: This review summarizes the current knowledge of protein and nucleic acid interactions with water, with a special focus on the biomolecular hydration layer. Recent developments in both experimental and computational methods that can be applied to the study of hydration structure and dynamics are reviewed, including software tools for the prediction and characterization of hydration layer properties. MAJOR CONCLUSIONS: In the last decade, important advances have been made in our understanding of the factors that determine how biomolecules and their aqueous environment influence each other. Both experimental and computational methods contributed to the gradually emerging consensus picture of biomolecular hydration. GENERAL SIGNIFICANCE: An improved knowledge of the structural and thermodynamic properties of the hydration layer will enable a detailed understanding of the various biological processes in which it is involved, with implications for a wide range of applications, including protein-structure prediction and structure-based drug design.
References provided by Crossref.org
From Gas to Solution: The Changing Neutral Structure of Proline upon Solvation
Knowledge-based prediction of DNA hydration using hydrated dinucleotides as building blocks
What Does Time-Dependent Fluorescence Shift (TDFS) in Biomembranes (and Proteins) Report on?
Structural alphabets for conformational analysis of nucleic acids available at dnatco.datmos.org