Abstract
The mechanisms by which regulatory proteins discern specific target DNA sequences remain a major area of inquiry. Detailed knowledge of the function, structure, dynamics, kinetics, and energetics of the interaction of a particular protein with both nonspecific and cognate DNA sequences is critical. To date, lactose repressor (lac) is the only protein-DNA system for which the complete recognition pathway has been structurally and dynamically characterized. A summary is given of how NMR recognition and how the knowledge that has become available through studies in the literature can be combined to give an unprecedented insight into the intricate interactions between proteins and DNA.
Original language | English (US) |
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Pages (from-to) | 3567-3586 |
Number of pages | 20 |
Journal | Chemical Reviews |
Volume | 104 |
Issue number | 8 |
DOIs | |
State | Published - Aug 1 2004 |