Fig. 3: Kinetics recorded using the temperature-jump source for exemplary biological systems.
From: Studying biomolecular folding and binding using temperature-jump mass spectrometry
a–c the formation of a self-complementary DNA duplex (20 µM d(CGT AAA TTT ACG) in 100 mM TMAA). M and D denote the mononer and duplex, respectively; d–f the binding of a ligand to a protein (5 µM Carbonic Anhydrase II (PDB ID: 1CA250) with 5 µM 4-carboxybenzene sulfonamide in 10 mM NH4OAc). CA and L denote Carbonic Anhydrase II and ligand, respectively; g–i the folding of a protein (10 µM Ribonuclease A (PDB ID: 5RSA80) in 100 mM NH4OAc at pH 2.75). RNase denotes Ribonuclease A; j–l the dissociation of a collagen peptide triple helix into monomers (40 µM [POG]8 collagen peptide (PDB ID: 1CGD54) in 10 mM NH4OAc). M and T denote monomer and trimer, respectively. The vertical error bars in f are the standard deviation obtained from the quantification on different charge states (12+, 11+, 10+, and 9+, n = 4). The reproducibility of the experiment is discussed in the Discussion section. The errors on the rate constants are the standard deviations from the fitting. Source data are provided as a Source Data file.
