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Detection and Identification of Protein‐Phosphorylation Sites in Histidines through HNP Correlation Patterns
Author(s) -
Himmel Sebastian,
Wolff Sebastian,
Becker Stefan,
Lee Donghan,
Griesinger Christian
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201003965
Subject(s) - phosphorylation , identification (biology) , pep group translocation , chemistry , phosphotransferase , computer science , information retrieval , computational biology , biochemistry , biology , gene , escherichia coli , botany
Three not of a kind : A NMR HNP experiment can distinguish between all three possible single‐ and double‐phosphorylated histidines without requiring p K a or chemical shift information (see picture). The method is tested on phosphorylated histidines and phosphocarrier protein HPr. It detects phosphorylation in phosphotransferase system regulation domain I (PRDI).

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