Biochemistry · 2008 · 90 citations · 69 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryProteomicsSpectroscopyMagnetic Resonance SpectroscopyProtein CharacterizationProtein StructureSpectroscopy Of BiomoleculesBiological ReductionismHigh-resolution Nuclear Magnetic Resonance SpectroscopyMagnetic Resonance Spectroscopy Of BiomoleculesNuclear Magnetic Resonance AnalysisNuclear Magnetic Resonance Spectroscopy
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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Virginia M.‐Y. Lee, Michel Goedert, John Q. Trojanowski · Annual Review of Neuroscience · 2001 · 2.4K citations
Protein Mobility in the Cytoplasm of <i>Escherichia coli</i>
Michael B. Elowitz, Michael G. Surette, P. E. Wolf et al. · Journal of Bacteriology · 1999 · 637 citations · Full text
Rajaram Swaminathan, Cailin Hoang, A.S. Verkman · Biophysical Journal · 1997 · 631 citations · Full text