[3] Structure and energy change in hemoglobin by hydrogen exchange labeling
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Cited by (36)
Elucidation of tRNA–cytochrome c interactions through hydrogen/deuterium exchange mass spectrometry
2017, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :The structural and conformational flexibility of cyt c enables rearrangement of the surface charge distribution and its affinity to the binding partner, thereby contributing to its versatile cellular functions [4]. The peptide amide H/D exchange technique has been employed to study the mechanisms of protein folding [24–26] and protein dynamics, domain structure, regional stability, and function [27,28]. The slowly exchanging peptide amide hydrogen is in equilibrium with the protons in the solvent [29,30].
Protein mechanics: How force regulates molecular function
2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :Based on structural information, Förster resonance energy transfer (FRET) experiments can yield rates on specified distances, also at the single molecule level, to interpret protein mechanics to elucidate allosteric effects [70–73]. Partial proteolysis in combination with gel electrophoresis [74] and hydrogen-deuterium exchange experiments in combination with mass spectrometry or NMR spectroscopy are mostly interpreted on the basis of complete protein structures, but can also combine structural information with thermodynamic data [75–78]. A broad range of theoretical methods further interpret the experimental data and build allosteric models via extensive data analysis.
Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry
2010, Journal of Biological ChemistryCitation Excerpt :The first class of peptides corresponded to five regions of MutS, which were found to be completely deuterated at the earliest time point examined, 10 s (Fig. 1B). These included the N terminus, regions of the clamp domain, the nucleotide-binding domain, and the flexible linker (residues 801–820) between the nucleotide-binding domain and the C-terminal dimerization/tetramerization domain (Fig. 1, C and D) (32), indicative of contiguous stretches of unstructured regions whose amides are exposed to solvent water (41, 42). The second class of peptides corresponded to five regions of MutS and showed little or no deuterium exchange, even at the longest time point examined, 3000 s.
Hydrogen Exchange and Mass Spectrometry: A Historical Perspective
2006, Journal of the American Society for Mass SpectrometryCitation Excerpt :Still, one cannot tell where in the protein these sensitive sites are. The development of a proteolytic fragmentation/HPLC separation method [22] was able to locate the positions of some of the allosterically sensitive sites at intermediate resolution [23]. The method is made possible by the fact that the HX halftime for unprotected amides is over 1 h at pH 2 to 3 and 0 °C (see Figure 1).
NMR study of the folding-unfolding mechanism for the thrombin-binding DNA aptamer d(GGTTGGTGTGGTTGG)
2005, Biophysical ChemistryHydrogen-Exchange Strategies Applied to Energetics of Intermediate Processes in Protein Folding
2004, Methods in Enzymology