Protein folding by mass spectrometry is the key to the structure and function of the protein. Protein folding by mass spectrometry has come to the forefront as a powerful biophysical method, which can shed light both on the structure and dynamics of proteins. Ligand binding can change the conformational state of the protein, and changes in the amino acid sequence of the protein can change both the structure and the activity, which may cause to disease states. Apart from the charge state distribution, we can also study protein folding and dynamics by MS by exchanging deuterium onto the amide groups of the peptide backbone. The exchange of amide protons for deuterium happens on the millisecond timescale. Exchange is much faster than the rate of closing.
Related journals of Protein Folding by Mass Spectrometry
Journal of Proteomics & Bioinformatics, Journal of Analytical & Bioanalytical Techniques, Journal of Chromatography & Separation Techniques, Journal of Chromatographic Science, Chromatography Research International and Journal of Liquid Chromatography and European Journal of Mass Spectrometry