Electrostatic Stabilization of a Native Protein Structure in the Gas Phase

摘要

Recently, a general picture has been proposed of how long, and to what extent, native protein structure can be retained in the gas phase. In particular, molecular dynamics simulations suggest that salt bridges and ionic hydrogen bonds on the protein surface can transiently stabilize the global fold shortly after desolvation. However, the use of native mass spectrometry for studying protein solution structure is still controversial, mostly because site-specific experimental gas-phase data is scarce.