Now showing items 1-1 of 1
Divalent ion-binding and thermal stability studies on rat [beta]-parvalbumin and the evidence of influential distant amino acid residues affecting CD site ion affinity
(University of Missouri--Columbia, 2011)
Parvalbumins (PVs) are vertebrate-specific proteins (Mr 12,000), which harbor two EF-hand motifs known as the CD and EF sites. Although the CD and EF sites are typically high-affinity sites, the mammalian [beta]-PV exhibits ...