Publication | Open Access
Protein Nuclear Magnetic Resonance under Physiological Conditions
90
Citations
69
References
2008
Year
Protein BiophysicsMagnetic ResonanceMolecular BiologyMagnetic Resonance ImagingProtein FoldingElectron Paramagnetic ResonanceProteomicsBiophysicsBiochemistrySolution Nmr SpectroscopyStructural BiologyMagnetic Resonance SpectroscopyNatural SciencesResonanceDynamic Nuclear PolarizationBiomolecular SpectroscopyProtein NmrCrowded ConditionsMedicinePhysiological Conditions
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.
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