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Hydrodynamic radius ladders of proteins
Author(s) -
Sharma Upma,
Carbeck Jeffrey D.
Publication year - 2005
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200410334
Subject(s) - radius , hydrodynamic radius , capillary action , peg ratio , measure (data warehouse) , self healing hydrogels , chemical physics , radius of gyration , electrophoresis , polyethylene glycol , polymer , capillary electrophoresis , materials science , chemistry , biological system , chromatography , polymer chemistry , computer science , organic chemistry , data mining , composite material , biology , computer security , finance , economics , copolymer
We introduce hydrodynamic radius ladders of proteins as a new tool to isolate and measure the role of hydrodynamic size on transport properties of proteins. Radius ladders are collections of derivatives of a protein that differ incrementally in number of polyethylene glycol (PEG) chains grafted to their surface. The addition of these chains causes the hydrodynamic size of the protein to increase. Capillary electrophoresis (CE) separates these derivatives into individual peaks or “rungs” of a ladder composed of proteins that have the same number of PEG chains, and provides a way to measure the values of hydrodynamic radius of proteins that constitute the rungs of the ladder. We demonstrate the utility of this approach by measuring the partitioning of radius ladders into polymer hydrogels. The combination of radius ladders and CE produces a large amount of internally consistent data on hydrodynamic size. This technique will have applicability to the study of the role of hydrodynamic size on transport.