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Conformational changes in β-endorphin as studied by electrospray ionization mass spectrometry

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  • Part of this work was presented at the 48th ASMS Conference on Mass Spectrometry and Allied Topics held in Long Beach, CA, USA.

Abstract

Because of a wide range of physiological functions, the structure of β-endorphin (BE) is of great interest. In this study, conformational changes in BE induced by methanol are explored with electrospray ionization-mass spectrometry (ESI-MS). Differences in the charge-state distribution (CSD) and the extent of hydrogen/deuterium (H/D) exchange were used to monitor the conformational changes. The latter experiments were conducted via time-resolved ESI-MS in a continuous-flow apparatus. Both these techniques demonstrate that BE exists in a random coil open structure in aqueous media, but it acquires a more compact conformation with increased concentration of methanol. The H/D exchange experiments reveal that BE forms 61% α-helix in mixed solvents. Copyright © 2001 John Wiley & Sons, Ltd.

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