Literature DB >> 518923

Calcium and magnesium binding by parvalbumin. A proton magnetic resonance spectral study.

W J Birdsall, B A Levine, R J Williams, J G Demaille, J Haiech, J F Pechere.   

Abstract

Proton magnetic resonance spectroscopy has been used to monitor the kinetics and nature of the conformational transitions induced by binding of calcium and magnesium to carp parvalbumin. Rate constants have been determined for the exchange between the cation dependent conformational states of the protein in solution. These data enable a description of the kinetics and mechanism controlling the calcium flux in vivo during contraction.

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Year:  1979        PMID： 518923     DOI： 10.1016/s0300-9084(79)80268-0

Source DB:  PubMed          Journal:  Biochimie        ISSN： 0300-9084            Impact factor:   4.079


  2 in total

1.  Conformational changes induced by binding of bivalent cations to oncomodulin, a paravalbumin-like tumour protein.

Authors:  J P MacManus; A G Szabo; R E Williams
Journal:  Biochem J       Date:  1984-05-15       Impact factor: 3.857

Review 2.  Ion binding to calmodulin. A comparison with other intracellular calcium-binding proteins.

Authors:  M C Kilhoffer; J Haiech; J G Demaille
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396
  2 in total

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