In this paper, we have demonstrated an Er-doped ultrafast laser with a single mode fiber-gradient index multimode fiber-single mode fiber(SMF-GIMF-SMF, SMS) structure as saturable absorber(SA), which can generate not ...In this paper, we have demonstrated an Er-doped ultrafast laser with a single mode fiber-gradient index multimode fiber-single mode fiber(SMF-GIMF-SMF, SMS) structure as saturable absorber(SA), which can generate not only stable single-pulse state, but also special mode-locked pulses with the characteristics of high energy and noisy behaviors at proper pump power and cavity polarization state. In addition, we have deeply investigated the real-time spectral evolutions of the mode-locked pulses through the dispersive Fourier transformation(DFT) technique. It can be found that the pulse regime can actually consist of a lot of small noise pulses with randomly varying intensities. We believe that these results will further enrich the nonlinear dynamical processes in the ultrafast lasers.展开更多
The single-chain elasticity of a completely unfolded protein （027）8, modules of human cardiac titin） is studied in different liquid environments by the atomic force microscopy （AFM）-based single molecule force sp...The single-chain elasticity of a completely unfolded protein （027）8, modules of human cardiac titin） is studied in different liquid environments by the atomic force microscopy （AFM）-based single molecule force spectroscopy （SMFS）. The experimental results show that there is a clear deviation between the force curves obtained in the aqueous and nonaqueous environments. Such a deviation can be attributed to the additional energy consumed by the rearrangement of the bound water molecules around the chain of the completely unfolded （I27）s chain upon stretching in aqueous solution, which is very similar to the partial dehydration process from a denatured/unfolded to a native/folded protein. Through the analysis of the free energy changes involved in protein folding, we conclude that it is due to the weak disturbance of water molecules and the special backbone structures of proteins that the self-assembly of proteins can be achieved in physiological conditions. We speculate that water is likely to be an important criterion for the selection of self-assembling macromolecules in the prebiotic chemical evolution.展开更多
基金supported by the Guangdong Basic and Applied Basic Research Foundation (No.2023A1515010093)the Shenzhen Fundamental Research Program (Stable Support Plan Program)(Nos.JCYJ20220809170611004, 20231121110828001 and 20231121113641002)the National Taipei University of Technology-Shenzhen University Joint Research Program (No.2024001)。
文摘In this paper, we have demonstrated an Er-doped ultrafast laser with a single mode fiber-gradient index multimode fiber-single mode fiber(SMF-GIMF-SMF, SMS) structure as saturable absorber(SA), which can generate not only stable single-pulse state, but also special mode-locked pulses with the characteristics of high energy and noisy behaviors at proper pump power and cavity polarization state. In addition, we have deeply investigated the real-time spectral evolutions of the mode-locked pulses through the dispersive Fourier transformation(DFT) technique. It can be found that the pulse regime can actually consist of a lot of small noise pulses with randomly varying intensities. We believe that these results will further enrich the nonlinear dynamical processes in the ultrafast lasers.
基金financially supported by the National Natural Science Foundation of China(Nos.21574106 and 21604074)the Sichuan Province Youth Science and Technology Innovation Team(Nos.2016TD0026 and 2017JQ0009)
文摘The single-chain elasticity of a completely unfolded protein （027）8, modules of human cardiac titin） is studied in different liquid environments by the atomic force microscopy （AFM）-based single molecule force spectroscopy （SMFS）. The experimental results show that there is a clear deviation between the force curves obtained in the aqueous and nonaqueous environments. Such a deviation can be attributed to the additional energy consumed by the rearrangement of the bound water molecules around the chain of the completely unfolded （I27）s chain upon stretching in aqueous solution, which is very similar to the partial dehydration process from a denatured/unfolded to a native/folded protein. Through the analysis of the free energy changes involved in protein folding, we conclude that it is due to the weak disturbance of water molecules and the special backbone structures of proteins that the self-assembly of proteins can be achieved in physiological conditions. We speculate that water is likely to be an important criterion for the selection of self-assembling macromolecules in the prebiotic chemical evolution.
