Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.
Proc Natl Acad Sci U S A. 2011 Jun 28;108(26):10396-9. doi: 10.1073/pnas.1103854108. Epub 2011 Jun 13.
Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when spinning is stopped, allowing one to study them in both conditions. Transiently sedimented proteins can be considered a novel phase as far as NMR is concerned. NMR of transiently sedimented molecules under fast magic angle spinning has the advantage of overcoming protein size limitations of solution NMR without the need of sample crystallization/precipitation required by solid-state NMR.
在典型的超速离心速度下，溶液中的相对较大的蛋白质在 NMR 转子中旋转，会在转子壁上沉降。沉降的蛋白质提供高质量类似于固态的 NMR 谱，适用于结构研究。当停止旋转时，蛋白质完全恢复到原始的溶液状态，允许在两种状态下研究它们。瞬态沉降的蛋白质在 NMR 方面可以被认为是一种新的相。在快速魔角旋转下，瞬态沉降分子的 NMR 具有克服溶液 NMR 中蛋白质大小限制的优势，而无需固体 NMR 所需的样品结晶/沉淀。
