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The Most Stable Protein–Ligand Complex: Applications for One‐Step Affinity Purification and Identification of Protein Assemblies
Author(s) -
Giese Christoph,
Zosel Franziska,
Puorger Chasper,
Glockshuber Rudi
Publication year - 2012
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.201108747
Subject(s) - identification (biology) , ligand (biochemistry) , computational biology , computer science , multiprotein complex , chemistry , combinatorial chemistry , information retrieval , biology , biochemistry , botany , receptor , gene
An alternative to tagging : The thermodynamically most stable protein–ligand complex known to date ( K D =1.5×10 −20 M ) consists of the two components FimGt and DsF, portions of two different subunits of the type 1 pilus protein complex. The first technical applications of this new complex are the single‐step purification and identification of multiprotein complexes from cell extracts.