DIR Studies of Proteins

2D-IR correlation spectroscopy has become a popular tool in the analysis of protein spectra since they gives rise to broad bands and the application of an external perturbation produces complex phenomena. It has been used to study the correlation of the amide bands and the assignment of the different band components to secondary structure (Arrondo et al. 2004). It has also been applied to analyse the kinetics of hydrogen-deuterium exchange in order to study solvent accessibility and the flexibility of the protein (Nabet and Pezolet 1997; Meskers et al. 1999). Protein unfolding and aggregation are also targets for the use of 2D-IR correlation spectroscopy since besides the analysis provided by synchronous maps, the asynchronous maps give an idea of the hierarchical order of events.

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