Protein structural dynamics at the gas/water interface examined by hydrogen exchange mass spectrometry

Protein Science : a Publication of the Protein Society
Yiming Xiao, Lars Konermann

Abstract

Gas/water interfaces (such as air bubbles or foam) are detrimental to the stability of proteins, often causing aggregation. This represents a potential problem for industrial processes, for example, the production and handling of protein drugs. Proteins possess surfactant-like properties, resulting in a high affinity for gas/water interfaces. The tendency of previously buried nonpolar residues to maximize contact with the gas phase can cause significant structural distortion. Most earlier studies in this area employed spectroscopic tools that could only provide limited information. Here we use hydrogen/deuterium exchange (HDX) mass spectrometry (MS) for probing the conformational dynamics of the model protein myoglobin (Mb) in the presence of N(2) bubbles. HDX/MS relies on the principle that unfolded and/or highly dynamic regions undergo faster deuteration than tightly folded segments. In bubble-free solution Mb displays EX2 behavior, reflecting the occurrence of short-lived excursions to partially unfolded conformers. A dramatically different behavior is seen in the presence of N(2) bubbles; EX2 dynamics still take place, but in addition the protein shows EX1 behavior. The latter results from interconversion of the native stat...Continue Reading

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Citations

Jul 7, 2015·The Journal of Physical Chemistry. B·Jacob WittenSheila S Jaswal
May 22, 2021·Frontiers in Chemistry·Xuefei WangShaoyong Lu
Apr 10, 2018·The Journal of Physical Chemistry. B·Yohko F YanoTadashi Matsushita

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