| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929071 | Biochemical and Biophysical Research Communications | 2012 | 6 Pages |
Abstract
⺠Structural difference between Ca2+- and Mg2+-loaded state of parvalbumin was studied. ⺠Ca2+- and Mg2+-bound forms of pike β-parvalbumin differ significantly. ⺠Cation-induced conformational changes are identical in the homologous α-isoform. ⺠Difference of spectral response on Ca2+/Mg2+ binding by β-parvalbumin is explained.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Anush G. Bakunts,