Ultrafast Vibrational Dynamics of Membrane-Bound Peptides at the Lipid Bilayer/Water Interface
Ultrafast Vibrational Dynamics of Membrane-Bound Peptides at the Lipid Bilayer/Water Interface
复制标题
脂质双层/水界面处膜结合肽的超快振动动力学
DOI：
10.1002/anie.201706996
复制
发表时间：
2017-10-09
影响因子：
16.6
通讯作者：
Ye, Shuji
中科院分区：
文献类型：
--
作者：
Tan, Junjun;Zhang, Baixiong;Ye, Shuji
Vibrational energy transfer (VET) of proteins at cell membrane plays critical roles in controlling the protein functionalities, but its detection is very challenging. By using a surface-sensitive femtosecond time-resolved sum-frequency generation vibrational spectroscopy with infrared pump, the detection of the ultrafast VET in proteins at cell membrane has finally become possible. The vibrational relaxation time of the N-H groups is determined to be 1.70(+/- 0.05)ps for the -helix located in the hydrophobic core of the lipid bilayer and 0.9(+/- 0.05)ps for the membrane-bound beta-sheet structure. The N-H groups with strong hydrogen bonding gain faster relaxation time. By pumping the amideA band and probing amideI band, the vibrational relaxation from N-H mode to C=O mode through two pathways (direct coupling and through intermediate states) is revealed. The ratio of the pathways depends on the NHO=C hydrogen-bonding strength. Strong hydrogen bonding favors the coupling through intermediate states.
