Solution thermochemistry of concanavalin A tetramer conformers measured by variable-temperature ESI-IMS-MS.

ABSTRACT: Variable-temperature nano-electrospray ionization coupled with ion mobility spectrometry-mass spectrometry is used to investigate the thermal denaturation of the tetrameric protein concanavalin A. As the solution temperature is increased, changes in mass spectra and collision cross section distributions provide evidence for discrete structural changes that occur at temperatures that are ~40 to 50 degrees below the temperature required for tetramer dissociation. The subtle structural changes are associated with four distinct tetramer conformations with unique melting temperatures. Gibbs-Helmholtz analysis of the free energies determined with respect to the most abundant "native" state yields heat capacities of ΔC_p = 1.6 ± 0.3, -2.2 ± 0.4, and -2.9 ± 1.6 kJ·K^-1·mol

SUBMITTER: El-Baba TJ 

PROVIDER: S-EPMC7100878 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature