B. Prêcheur

Characterization of a synthetic calmodulin-binding peptide derived from Bacillus anthracis adenylate cyclase.

O. Bârzu, F. Blanco, C. Craescu, 1993, The Journal of biological chemistry.

1H and 15N NMR characterization of free and bound states of an amphiphilic peptide interacting with calmodulin.

O. Bârzu, C. Craescu, J. Mispelter, 1992, Biochemistry.

NMR and circular dichroic studies of the solution structure of conformationally constrained antigenic peptides.

C. Craescu, H. Gras-masse, B. Prêcheur, 1994, European journal of biochemistry.

NMR and circular dichroic studies on the solution conformation of a synthetic peptide derived from the calmodulin-binding domain of Bordetella pertussis adenylate cyclase.

O. Bârzu, C. Craescu, B. Prêcheur, 1991, European journal of biochemistry.

NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.

R. Riek, G. Wider, K. Wüthrich, 1999, Journal of molecular biology.

Nereis sarcoplasmic Ca2+‐binding protein has a highly unstructured apo state which is switched to the native state upon binding of the first Ca2+ ion

J. Cox, C. Craescu, J. Mispelter, 1996, FEBS letters.