Protein Nuclear Magnetic Resonance under Physiological Conditions

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• 作者：Gary J. Pielak ; Conggang Li ; Andrew C. Miklos ; Alexander P. Schlesinger ; Kristin M. Slade ; Gui-Fang Wang ; Imola G. Zigoneanu
• 刊名：Biochemistry
• 出版年：2009
• 出版时间：January 20, 2009
• 年：2009
• 卷：48
• 期：2
• 页码：226-234
• 全文大小：202K
• 年卷期：v.48,no.2(January 20, 2009)
• ISSN：1520-4995

文摘

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.