Abstract
Proteins are characterized by a number of slow processes (time constants > 10-4 sec), which are thought to be associated with cooperative motions of large groups of atoms. Structural studies of proteins have led to the characterization of large-scale, concerted conformational changes in a number of systems. Such conformational changes are often coupled with ligand binding or covalent modification of the protein, making them amenable to experimental manipulation. It is usually possible to correlate these large-scale motions with the biological or enzymatic function of the protein. In some cases, the conformational changes appear to be coupled with perturbations of spectroscopic probes that provide some information about the time scales of the perturbation, although it is rarely possible to assign rates to the large-scale motions themselves.
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