Neutralization of surface charges markedly affects the properties of bovine calbindin D9k.

Abstract

Calbindin D9k constitutes an attractive model system for exploring the relationships between structure, dynamics and function in the EF-hand family of proteins. It is the smallest protein known (Mr ≈ 8,500; 75 a.a:s) with a pair of EF-hand Ca2+-binding sites and its structure resembles closely the globular domains of the homologous proteins calmodulin, parvalbumin and skeletal muscle troponin C. [1,7]. The schematic structure of calbindin is shown in Fig. 1.