Arumugam S, Pascal S, North C L, Hu W, Lee K C, Cotten M, Ketchem R R, Xu F, Brenneman M, Kovacs F, Tian F, Wang A, Huo S, Cross T A
Center for Interdisciplinary Magnetic Resonance at the National High Magnetic Field Laboratory, Institute of Molecular Biophysics, Florida State University, Tallahassee, 32306, USA.
Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):5872-6. doi: 10.1073/pnas.93.12.5872.
Functional regulation of proteins is central to living organisms. Here it is shown that a nonfunctional conformational state of a polypeptide can be kinetically trapped in a lipid bilayer environment. This state is a metastable structure that is stable for weeks just above the phase transition temperature of the lipid. When the samples are incubated for several days at 68 degrees C, 50% of the trapped conformation converts to the minimum-energy functional state. This result suggests the possibility that another mechanism for functional regulation of protein activity may be available for membrane proteins: that cells may insert proteins into membranes in inactive states pending the biological demand for protein function.
蛋白质的功能调节对生物体至关重要。本文表明，多肽的一种无功能构象状态可在动力学上被困于脂质双层环境中。这种状态是一种亚稳结构，在略高于脂质相变温度的条件下可稳定存在数周。当样品在68摄氏度下孵育数天时，50%被困构象会转变为最低能量功能状态。这一结果表明，膜蛋白可能存在另一种蛋白质活性功能调节机制：细胞可能将蛋白质以无活性状态插入膜中，等待对蛋白质功能的生物学需求。
