Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety

2012 ◽  
Vol 116 (14) ◽  
pp. 4181-4191 ◽  
Author(s):  
N. Regner ◽  
T. T. Herzog ◽  
K. Haiser ◽  
C. Hoppmann ◽  
M. Beyermann ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Ultrafast Spectroscopy ◽  
Peptide Moiety

scholarly journals Empirical rules of molecular photophysics in the light of ultrafast spectroscopy

2015 ◽  
Vol 87 (6) ◽  
pp. 525-536 ◽  
Author(s):  
Majed Chergui
Keyword(s):  
Structural Dynamics ◽  
Ultrafast Spectroscopy ◽  
Molecular Complexes ◽  
Ultrafast Laser ◽  
Intersystem Crossing ◽  
Spin Orbit Coupling ◽  
Ultrafast Laser Spectroscopy ◽  
Coupling Constant ◽  
Heavy Atoms ◽  
Common Observation

AbstractThe advent of ultrafast laser spectroscopy has allowed entirely new possibilities for the investigation of the ultrafast photophysics of inorganic metal-based molecular complexes. In this review we show different regimes where non-Kasha behavior shows up. We also demonstrate that while ultrafast intersystem crossing is a common observation in metal complexes, the ISC rates do not scale with the magnitude of the spin-orbit coupling constant. Structural dynamics and density of states play a crucial role in such ultrafast ISC processes, which are not limited to molecules containing heavy atoms.

scholarly journals Correlating structural dynamics and catalytic activity of AgAu nanoparticles with ultrafast spectroscopy and all-atom molecular dynamics simulations

2018 ◽  
Vol 208 ◽  
pp. 269-286 ◽  
Author(s):  
G. F. Ferbonink ◽  
T. S. Rodrigues ◽  
D. P. dos Santos ◽  
P. H. C. Camargo ◽  
R. Q. Albuquerque ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Structural Dynamics ◽  
Ultrafast Spectroscopy ◽  
Surface Segregation ◽  
Core Shell ◽  
Hollow Core ◽  
Phonon Coupling ◽  
Electron Phonon Coupling ◽  
Equilibrium Structures ◽  
Dynamics Simulations

Electron–phonon coupling times, equilibrium structures and surface segregation as a function of hollow core–shell AgAu nanoparticle composition.

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

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