title: Protein nuclear magnetic resonance under physiological conditions.
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.
authors.affiliation: Department of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA. gary_pielak@unc.edu
authors.forename: Gary J
authors.initials: GJ
authors.lastname: Pielak
authors.forename: Conggang
authors.initials: C
authors.lastname: Li
authors.forename: Andrew C
authors.initials: AC
authors.lastname: Miklos
authors.forename: Alexander P
authors.initials: AP
authors.lastname: Schlesinger
authors.forename: Kristin M
authors.initials: KM
authors.lastname: Slade
authors.forename: Gui-Fang
authors.initials: GF
authors.lastname: Wang
authors.forename: Imola G
authors.initials: IG
authors.lastname: Zigoneanu
mesh_terms: D002244:Carbon / Q000737:chemistry; D003903:Deuterium / Q000737:chemistry; D004058:Diffusion; D009584:Nitrogen / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*
chemical_list: D011506:Proteins; D002244:Carbon; D003903:Deuterium; D009584:Nitrogen