Measuring hydrogen exchange in proteins by selective water saturation in 1H–15N SOFAST/BEST-type experiments: advantages and limitations - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Biomolecular NMR Année : 2014

Measuring hydrogen exchange in proteins by selective water saturation in 1H–15N SOFAST/BEST-type experiments: advantages and limitations

Fichier non déposé

Dates et versions

hal-01321278 , version 1 (25-05-2016)

Identifiants

Citer

Enrico Rennella, Zsófia Sólyom, Bernhard Brutscher. Measuring hydrogen exchange in proteins by selective water saturation in 1H–15N SOFAST/BEST-type experiments: advantages and limitations. Journal of Biomolecular NMR, 2014, 60 (2-3), pp.99-107. ⟨10.1007/s10858-014-9857-8⟩. ⟨hal-01321278⟩
33 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More