Rafael Bruschweiler | Homepage

Professor of Chemistry & Biochemistry

Research Interests

Main Focus

Research in the Bruschweiler Laboratory foucses on the structural dynamics of proteins, structural genomics, covariance NMR spectroscopy and quantum information processing.

Structural Dynamics of Proteins

We employ nuclear magnetic resonance spectroscopy (NMR), which is a very powerful tool that measures the strengths, directions, and temporary fluctuations of magnetic interactions at the location of essentially each atom in the protein by means of chemical shifts, spin-spin couplings, and spin relaxation times, respectively. This information, in combination with suitable models, provides unique insight into the structural dynamics of the protein on widely different time scales ranging from seconds to tens of picoseconds. We are developing new protocols for the comprehensive analysis of experimental data using computational and database derived models and apply them to different protein systems. The emerging view of protein dynamics often (but not always) involves motional correlation effects across the protein and thereby also provides access to the protein's conformational entropy, which is one of the dominant driving forces of protein function.

Covariance NMR Specroscopy

To shorten the NMR measurement time for multi-dimensional NMR spectra and to facilitate their analysis and interpretation, we are developing Covariance NMR Spectroscopy, which represents an NMR spectrum in terms of a covariance matrix calculated from a selected set of one-dimensional NMR spectra. The covariance spectrum can then be subjected to principal component analysis (PCA) that directly provides dominant correlation information. Application to chemical mixtures, for example, allows the easy identification of individual chemical components, which may become useful in the emerging biomedical field of metabolomics.

Teaching

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