Rief M, Gautel M, Gaub H E
Stanford University School of Medicine, CA, USA.
Adv Exp Med Biol. 2000;481:129-36; discussion 137-41. doi: 10.1007/978-1-4615-4267-4_8.
AFM-based Single Molecule Force Spectroscopy provides a new tool for probing the mechanical properties of single molecules. In this chapter we show that the unfolding forces of single protein domains can be directly measured. Unfolding forces give new insight into protein stability that cannot be deduced from thermodynamic measurements. A comparison between the unfolding forces measured in Ig domains of the muscle protein titin and those measured in fibronectin Type III domains reveals an extraordinarily high stability of titin domains.
基于原子力显微镜的单分子力谱为探测单分子的力学性质提供了一种新工具。在本章中,我们展示了可以直接测量单个蛋白质结构域的解折叠力。解折叠力为蛋白质稳定性提供了新的见解,这是无法从热力学测量中推断出来的。对肌肉蛋白肌联蛋白免疫球蛋白结构域中测得的解折叠力与纤连蛋白III型结构域中测得的解折叠力进行比较,结果显示肌联蛋白结构域具有极高的稳定性。