Protein nuclear magnetic resonance under physiological 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.
Pielak
Gary J
GJ
Department of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA. gary_pielak@unc.edu
Li
Conggang
C
Miklos
Andrew C
AC
Schlesinger
Alexander P
AP
Slade
Kristin M
KM
Wang
Gui-Fang
GF
Zigoneanu
Imola G
IG
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*
D011506:Proteins; D002244:Carbon; D003903:Deuterium; D009584:Nitrogen