Conformational Dynamics in Weakly Structured Regions of Proteins

3 Conformational Dynamics in Weakly Structured Regions of Proteins 

The conventional bottom-up LC workflow was adapted for this type of experiment by Rist et al. in 2005 and demonstrated on an Escherichia coli heat shock protein that included a weakly structured C-terminal helix bundle domain [6]. Using labeling times from 100 ms to 30 s, the authors were able to identify protection factors ranging from 10 to 36. This study was the first report of a fully automated system for bottom-up millisecond HX and the first to propose expected versus observed millisecond exchange as a way to validate crystal structures (see Section 5.3.2). 

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