A systematic method for analysing the protein hydration structure of T4 lysozyme

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191799" target="_blank" >RIV/00216208:11310/13:10191799 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/13:00396329
Result on the web
<a href="http://dx.doi.org/10.1002/jmr.2290" target="_blank" >http://dx.doi.org/10.1002/jmr.2290</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/jmr.2290" target="_blank" >10.1002/jmr.2290</a>

Result language
angličtina
Original language name
A systematic method for analysing the protein hydration structure of T4 lysozyme
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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