Conformational analysis of dynorphin A (1-13) using hydrogen-deuterium exchange and tandem mass spectrometry.
Trifluoroethanol (TFE)-induced conformational changes in dynorphin A (1-13) were investigated using charge-state distribution (CSD) and hydrogen-deuterium exchange (HDX), combined with electrospray ionization (ESI) mass spectrometry (MS). Individual amino acids involved in secondary structural elements were identified by collision-induced dissociation-tandem mass spectrometry (MS/MS). It was observed that dynorphin A (1-13) largely exists in an unfolded conformation and a folded structure in increasing concentrations of TFE. In 50% TFE, it forms an alpha-helix that encompasses residues 1-9 and remains flexible from residues 10 to 13.
Cai
Xianmei
X
Department of Chemistry, The University of Memphis, Memphis, TN 38152, USA.
Dass
Chhabil
C
D041961:Deuterium Exchange Measurement; D004399:Dynorphins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation / Q000187:drug effects; D053719:Tandem Mass Spectrometry; D014270:Trifluoroethanol / Q000494:pharmacology
D010446:Peptide Fragments; C026843:dynorphin (1-13); D004399:Dynorphins; D014270:Trifluoroethanol