A systematic method for analysing the protein hydration structure of T4 lysozyme
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23996490
DOI
10.1002/jmr.2290
Knihovny.cz E-zdroje
- Klíčová slova
- X-ray crystallography, cluster algorithm, interaction enthalpy, protein hydration structure, water,
- MeSH
- bakteriofág T4 chemie enzymologie MeSH
- databáze proteinů MeSH
- molekulární modely MeSH
- muramidasa chemie MeSH
- termodynamika MeSH
- virové proteiny chemie MeSH
- voda chemie MeSH
- vodíková vazba MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- muramidasa MeSH
- virové proteiny MeSH
- voda 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.
Citace poskytuje Crossref.org
Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures
