Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry.
The binding of sodium ions to the transmembrane channel peptide gramicidin A has permitted the use of electrospray ionization mass spectrometry to study its conformation in different solvent environments. The mass spectra of the peptide in the various solvents suggest that different conformations of...
Main Authors: | Bouchard, M, Benjamin, DR, Tito, P, Robinson, C, Dobson, C |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2000
|
Similar Items
-
Influence of solvents on gramicidin a conformational interconversion
by: Bouchard, M, et al.
Published: (1998) -
COOPERATIVE ELEMENTS IN PROTEIN-FOLDING MONITORED BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
by: Hooke, S, et al.
Published: (1995) -
Mapping the structural characteristics of an ion channel in lipid bilayers: A H/D exchange MS/MS study of gramicidin A.
by: Bouchard, M, et al.
Published: (1999) -
Weighing the evidence for structure: electrospray ionization mass spectrometry of proteins.
by: Robinson, C, et al.
Published: (1995) -
AN INVESTIGATION INTO THE MECHANISM OF ELASTASE INHIBITION BY CEPHALOSPORINS USING ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
by: Aplin, R, et al.
Published: (1993)