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NMR spin relaxation spectroscopy is a proven method for characterization of the time-scales and amplitudes of intramolecular motions in proteins. In a typical NMR relaxation experiment, the significant contributions to ...

A widely held view with respect to the folding of single-domain proteins is that they are two-state. In other words, it is seemingly sufficient to invoke just two thermodynamic macrostates - folded and unfolded - to explain ...

Protein-induced bending of DNA plays an important role in regulating its transcription, replication, recombination, and packaging into nucleosomes. In particular, many general and gene-specific transcription factors bend ...

In this dissertation, we describe computational and theoretical study of backbone 15N chemical shieldings in peptides and proteins. Comprehensive density functional calculations have been performed on systems of different ...

In addition to the well known two-state folding scenario, the energy landscape theory of protein folding predicts the possibility of downhill folding under native conditions. This intriguing prediction was extended by ...