Intermediate trapping and laue X-ray diffraction: Potential for enzyme mechanism, dynamics, and inhibitor screening
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Cited by (21)
Coarse-grained free energy functions for studying protein conformational changes: A double-well network model
2007, Biophysical JournalCitation Excerpt :However, a molecular-level understanding of conformational changes requires sequential measurements of protein structure during a transition event. This challenge has motivated the development and use of cryo-electron microscopy (8–11), time-resolved x-ray (12–15), nuclear magnetic resonance (16,17), atomistic force spectroscopy (18,19), and single-molecule spectroscopy such as florescence energy transfer (20,21) to probe the dynamics of protein conformational changes. However, the spatial and temporal resolution of these measurements is still limited for describing protein conformational changes.
Crystallographic analysis of solvent-trapped intermediates of chymotrypsin
1999, Methods in EnzymologyNew results using Laue diffraction and time-resolved crystallography
1998, Current Opinion in Structural BiologyAn In Crystallo Reaction with an Engineered Cytochrome P450 Peroxygenase**
2024, Chemistry - A European Journal
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