@inbook{ef1ab8290e0f4ad8b9b66ab68000c708,
title = "Fluorescence measurements of Ca2+ binding to domain VI of calpain",
abstract = "The Ca2+ binding properties of calpain are of great interest, both biochemically in the wider context of EF-hand proteins, and physiologically, in the context of calpain regulation. There are two major parameters which one might wish to measure: the actual number of binding sites (n) and the binding constants for Ca2+. The latter is normally the macroscopic binding constant for Ca2+ of the molecule as a whole (Kd), or the microscopic binding constants for each of the EF-hands, but for cooperative binding these are much more difficult to measure. There is evidence of various kinds to suggest that Ca2+ binding causes conformational change in the whole molecule, and this forms the basis for measuring Ca2+ binding by means of changes in fluorescence.",
keywords = "Rats, Animals, Calcium, Spectrometry, Fluorescence, Recombinant Proteins, Kinetics, Calpain, Protein Structure, Tertiary, Protein Structure, Quaternary, Binding Sites",
author = "Arthur, {J. Simon C.} and Elce, {John S.}",
year = "2000",
doi = "10.1385/1-59259-050-0:121",
language = "English",
isbn = "9780896036321",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "121--127",
editor = "Elce, {John S.}",
booktitle = "Calpain Methods and Protocols",
address = "United States",
edition = "Part II",
}