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Molecular dynamics of biological macromolecules: A brief history and perspective
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The ensemble nature of proteins has far-reaching implications for understanding basic natural protein functions such as ligand binding, enzyme catalysis, and allostery. By extension, an understanding of protein dynamics should lead to improvements in protein engineering and rational drug design.

This includes enzymes such as dihydrofolate reductase DHFR , which is essential in all organisms for nucleotide biosynthesis. It is also the target for drugs used to treat human cancers and antibiotics and is therefore an excellent system for studying protein-drug interactions.

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These are found throughout nature in a variety of contexts and are widespread as signal transduction modules in higher eukaryotes. PDZ domains specialize in binding C-terminal sequences of signaling enzymes, transmembrane receptors, proteases, etc.

Macromolecules - Classes and Functions

They are also recognized as models for intramolecular communication. Other ongoing projects in the lab are directed at the role of protein dynamics in allostery and their distinguishing features from non-allosteric proteins. How does Lee characterize protein dynamics? Thee preferred method is heteronuclear NMR spectroscopy, which is uniquely suited to study both structure and dynamics in proteins and other biological macromolecules.

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A major advantage of NMR is that spectroscopic probes are distributed uniformly throughout the biomolecule , such as NH or CH atom pairs, providing large amounts of molecular information. To gain information on protein dynamics, NMR spin relaxation is highly sensitive to molecular motion over a range of timescales. The Physics and Psychophysics of Music.

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