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Back Cover: The Scaffold Design of Trivalent Chelator Heads Dictates Affinity and Stability for Labeling His‐tagged Proteins in vitro and in Cells (Angew. Chem. Int. Ed. 38/2018)
Author(s) -
Gatterdam Karl,
Joest Eike F.,
Gatterdam Volker,
Tampé Robert
Publication year - 2018
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.201808284
Subject(s) - nitrilotriacetic acid , scaffold , chelation , chemistry , in vitro , fluorophore , scaffold protein , histidine , biophysics , int , combinatorial chemistry , fluorescence , biochemistry , amino acid , signal transduction , biology , organic chemistry , biomedical engineering , computer science , operating system , medicine , physics , quantum mechanics
TrisNTA chelators consist of three metal‐chelating N‐nitrilotriacetic acids (NTAs) connected by a scaffold structure. Coupled to a fluorophore or other reporter, tris NTAs can be used as a probe for live‐cell labeling of histidine‐tagged proteins. In their Communication on page 12395 ff., R. Tampé et al. report large differences in affinity and stability between linear, dendritic, and cyclic scaffolds, and clarify which tris NTA scaffold is superior for in vitro and cellular applications.