Résumé
The structural study of proteins by NMR involves various key steps such as the preparation of biological macromolecules, the assignment of the obtained NMR spectra or the reconstruction of a structure via molecular modeling steps. Part of my work is related to the NMR structural study of two thioredoxins. I carried out the study of Triticum Aestivum thioredexin h (127 residues) and the reconstruction of a possible model by structural homology. Another molecular modeling study (molecular dynamics in water) was performed on a mutant of the Escherichia coli thioredoxin (108 residues) to observe the effects of the mutation, then a more complete NMR study was performed to try to verify the results observed in modeling. I also focused on the development of a method for reconstructing molecular structures using distance geometry and not including the attribution step.