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The research team of Professor Luo Yi of hefei Microscale Material Science National Laboratory, Quantum Innovation Research Institute and Department of Chemical Physics of China University of Science and Technology made progress in the vibrational energy transfer of membrane protein interface.
The team revealed the rate and pathways of energy transfer of the vibration of the proteinamide key skeleton in the biofilm interface, published in the German Journal of Applied Chemistry under the title Ultrafast Vibrational Dynamics of Membrane-Bound Peptides at the Lipid Bilayer/Water Interface.
electron and energy transfer processes are known as the heart of chemical reaction dynamics, determining all the initial steps of a chemical reaction.
Protein molecular energy transfer is essential for biochemical reactions and the normal functioning of physiological functions, and many physiological and cellular processes depend on the ultra-fast energy transfer processes of proteins, for example, the transmission of image changes and the transmission of variable communication are directly related to the transmission of energy along the protein skeleton.
rapid and effective energy transfer is a guarantee that the protein will remain operating normally over a very narrow temperature range.
therefore, understanding the energy transfer process of proteins in biofilm interface is the key to reveal the working mechanism of membrane proteins.
So far, there has been very limited understanding of the energy transfer of proteins (especially interface proteins), for example, how vibrational energy is transmitted within proteins, how it is associated with the transmission of image changes, how it leads to function, and whether vibrational energy transfer is a direct corelated transfer process.
Its roots lie in the fact that the energy transfer process involves excitation state dynamics in picosics or shorter time scales, and there is currently a lack of effective methods and data accumulation in the theoretical and experimental description of excitation state dynamics, especially interface excitation state dynamics.
recently, the leaf tree group independently set up a dynamic selection excitation - and frequency spectral detection of the fly-second time-resolution measurement system, its technical indicators reached the current international most advanced level.
The vibrational energy transfer rate of protein N-H on the biofilm in the water environment was measured for the first time by using a femtome infrared pulse with specific energy to select an N-H group that excites proteins on the biofilm, and monitoring the transient structural changes of the N-H substrate with femtome and frequency spectra (Figure 1).
By stimulating the N-H substrate to detect transient structural changes in the alamy key C-O, the researchers found that there are two ways to transmit vibrational energy from N-H to C-O: one is a direct NH-CO coupling, the other is N-H relaxation to a certain intermediate state (remembered as X-state), X-state and C-O coupling (Figure 2).
of the hydrogen bond determines the ratio of the two coupling pathways between N-H and C-O.
hydrogen bond, the higher the ratio of coupling, revealing the hydrogen bond effect on membrane protein energy transmission path and rate of the law. The
Leaf Tree Group is committed to developing and perfecting new technologies of high sensitivity, rapid identification, in-place real-time mark-free and frequency spectroscopy with interface selectivity, systematically studying the interface physics and chemistry of complex systems, and has now formed a set of relatively complete methods of complex molecular structure, interaction and dynamics of the characteristic interface.
the work has been funded by the Key and Surface Projects of the National Natural Science Foundation of China, the National Key Research and Development Program, the Central University Development Fund for The Important Directions of Projects, the Chinese Academy of Sciences, etc.
.