Protein Nuclear Magnetic Resonance under Physiological Conditions

Gary J. Pielak, Conggang Li, Andrew C. Miklos, Alexander P. Schlesinger, Kristin M. Slade, Gui-Fang Wang, Imola G. Zigoneanu

Biochemistry · 2008 · 90 citations · 69 references

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Abstract

Almost everything we know about protein biophysics comes from studies on purified proteins in dilute solution. Most proteins, however, operate inside cells where the concentration of macromolecules can be >300 mg/mL. Although reductionism-based approaches have served protein science well for more than a century, biochemists now have the tools to study proteins under these more physiologically relevant conditions. We review a part of this burgeoning postreductionist landscape by focusing on high-resolution protein nuclear magnetic resonance (NMR) spectroscopy, the only method that provides atomic-level information over an entire protein under the crowded conditions found in cells.

References

69