【摘 要】
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The mechanical stability of immunoglobulin protein domains in the force bearing muscle protein titin has been extensively studied.However, due to the presence of a large kinetic barrier to unfolding,
【机 构】
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Department of Physics,Xiamen University Mechanobi
【出 处】
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8th IUPAP International Conference on Biological Physics(第八届
论文部分内容阅读
The mechanical stability of immunoglobulin protein domains in the force bearing muscle protein titin has been extensively studied.However, due to the presence of a large kinetic barrier to unfolding, the free energy cost of unfolding of titin lg domains under mechanical force, $\Delta G(f)$, has not been determined.Using the 27th lg domain in the I-band of titin as a model system, we report the first direct measurement of its $\Delta G(f)$, determining a critical force of $f_c\sim 5.25 pN at which $\Delta G(f_c)=0$ and a transition rate in the order of $10^{-3}～s^{-1}$.In addition, a zero force value of $\Delta G(0)=8.7～k_B T$ is determined,which agrees with that reported from previous chemical denaturation studies.These results have important physiological implications, as they suggest that the conformations of titin lg domains can be significantly changed during low force, long duration of muscle stretching.
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