Abstract
The use of lanthanide energy transfer in the "rapid-diffusion limit" for probing the electrostatic properties of proteins has been investigated by measuring rates of energy transfer from Tb(III) chelates (having charges 1+, 0, and 1-) to the heme of sperm whale met(aquo)myoglobin, as a function of pH. The results are in good agreement with the predictions of a simple model involving the overall charge of the protein. The preparation of terbium(III) N,N′-bis(2-hydroxyethyl)-ethylenediaminediacetate, a new positively charged Tb(III) chelate similar in size and shape to negative terbium(III) ethylenediaminetetraacetate and neutral terbium(III) N-(2-hydroxyethyl)ethylenediaminetriacetate, is described.
Original language | English (US) |
---|---|
Pages (from-to) | 6247-6254 |
Number of pages | 8 |
Journal | Biochemistry |
Volume | 22 |
Issue number | 26 |
State | Published - 1983 |
ASJC Scopus subject areas
- Biochemistry