A systematic method for analysing the protein hydration structure of T4 lysozyme
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23996490
DOI
10.1002/jmr.2290
Knihovny.cz E-resources
- Keywords
- X-ray crystallography, cluster algorithm, interaction enthalpy, protein hydration structure, water,
- MeSH
- Bacteriophage T4 chemistry enzymology MeSH
- Databases, Protein MeSH
- Models, Molecular MeSH
- Muramidase chemistry MeSH
- Thermodynamics MeSH
- Viral Proteins chemistry MeSH
- Water chemistry MeSH
- Hydrogen Bonding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Muramidase MeSH
- Viral Proteins MeSH
- Water MeSH
A systematic method for the analysis of the hydration structure of proteins is demonstrated on the case study of lysozyme. The method utilises multiple structural data of the same protein deposited in the protein data bank. Clusters of high water occupancy are localised and characterised in terms of their interaction with protein. It is shown that they constitute a network of interconnected hydrogen bonds anchored to the protein molecule. The high occupancy of the clusters does not directly correlate with water-protein interaction energy as was originally hypothesised. The highly occupied clusters rather correspond to the nodes of the hydration network that have the maximum number of hydrogen bonds including both the protein atoms and the surrounding water clusters.
References provided by Crossref.org
Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures
