Mode specific vibrational relaxation in weakly bound binary complexes

1988 ◽  
Author(s):  
R. E. MIller
Keyword(s):  
Vibrational Relaxation ◽  
Weakly Bound ◽  
Binary Complexes

scholarly journals Does Oxygen Feature Chalcogen Bonding?

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3166 ◽  
Author(s):  
Pradeep R. Varadwaj
Keyword(s):  
Covalent Bond ◽  
Basis Set ◽  
General View ◽  
Weakly Bound ◽  
Binary Complexes ◽  
Covalently Bonded ◽  
Close Proximity ◽  
Correlation Consistent ◽  
Consistent Basis ◽  
Moller Plesset

Using the second-order Møller–Plesset perturbation theory (MP2), together with Dunning’s all-electron correlation consistent basis set aug-cc-pVTZ, we show that the covalently bound oxygen atom present in a series of 21 prototypical monomer molecules examined does conceive a positive (or a negative) σ-hole. A σ-hole, in general, is an electron density-deficient region on a bound atom M along the outer extension of the R–M covalent bond, where R is the reminder part of the molecule, and M is the main group atom covalently bonded to R. We have also examined some exemplar 1:1 binary complexes that are formed between five randomly chosen monomers of the above series and the nitrogen- and oxygen-containing Lewis bases in N2, PN, NH3, and OH2. We show that the O-centered positive σ-hole in the selected monomers has the ability to form the chalcogen bonding interaction, and this is when the σ-hole on O is placed in the close proximity of the negative site in the partner molecule. Although the interaction energy and the various other 12 characteristics revealed from this study indicate the presence of any weakly bound interaction between the monomers in the six complexes, our result is strongly inconsistent with the general view that oxygen does not form a chalcogen-bonded interaction.

Photochemical processes in weakly bound binary complexes

1991 ◽  
Vol 91 (6) ◽  
pp. 1193-1212 ◽  
Author(s):  
Masao. Takayanagi ◽  
Ichiro. Hanazaki
Keyword(s):  
Weakly Bound ◽  
Photochemical Processes ◽  
Binary Complexes

CRYO-Electron Microscopy of the Acto-Myosin-ATP Complex

1990 ◽  
Vol 48 (1) ◽  
pp. 248-249
Author(s):  
John Trinickt ◽  
Howard White
Keyword(s):  
Electron Microscopy ◽  
Atp Hydrolysis ◽  
Myosin Head ◽  
Bound State ◽  
Cross Linking ◽  
Weakly Bound ◽  
Cryo Electron Microscopy ◽  
Myosin Subfragment 1 ◽  
Attached State ◽  
High Fraction

The primary force of muscle contraction is thought to involve a change in the myosin head whilst attached to actin, the energy coming from ATP hydrolysis. This change in attached state could either be a conformational change in the head or an alteration in the binding angle made with actin. A considerable amount is known about one bound state, the so-called strongly attached state, which occurs in the presence of ADP or in the absence of nucleotide. In this state, which probably corresponds to the last attached state of the force-producing cycle, the angle between the long axis myosin head and the actin filament is roughly 45°. Details of other attached states before and during power production have been difficult to obtain because, even at very high protein concentration, the complex is almost completely dissociated by ATP. Electron micrographs of the complex in the presence of ATP have therefore been obtained only after chemically cross-linking myosin subfragment-1 (S1) to actin filaments to prevent dissociation. But it is unclear then whether the variability in attachment angle observed is due merely to the cross-link acting as a hinge.We have recently found low ionic-strength conditions under which, without resorting to cross-linking, a high fraction of S1 is bound to actin during steady state ATP hydrolysis. The structure of this complex is being studied by cryo-electron microscopy of hydrated specimens. Most advantages of frozen specimens over ambient temperature methods such as negative staining have already been documented. These include improved preservation and fixation rates and the ability to observe protein directly rather than a surrounding stain envelope. In the present experiments, hydrated specimens have the additional benefit that it is feasible to use protein concentrations roughly two orders of magnitude higher than in conventional specimens, thereby reducing dissociation of weakly bound complexes.

Double-Excitation Dynamics in m-LPPP probed with sub-20 fs Time Resolution

2003 ◽  
Vol 771 ◽  
Author(s):  
C. Gadermaier ◽  
G. Cerullo ◽  
C. Manzoni ◽  
U. Scherf ◽  
E.J.W. List ◽  
...  
Keyword(s):  
Vibrational Relaxation ◽  
Broad Band ◽  
Generation Efficiency ◽  
Exciton Dissociation ◽  
Charge Generation ◽  
Carrier Generation ◽  
Dissociation Probability ◽  
Ultrafast Relaxation ◽  
First Excited State ◽  
Differential Transmission

AbstractIn a novel modification of transient differential transmission spectroscopy, the first excited state S1 is reexcited via a second laser pulse towards a higher lying state Sn. The dynamics of the relaxation of this state Sn as well as the states created from Sn are revealed by a broad-band probe pulse.We find that the charge carrier generation efficiency from Sn is higher compared to S1. The push and probe durations below 20 fs enable the temporal resolution of the ultrafast relaxation of the Sn state and enables us to identify the two main contributions to enhanced charge generation from Sn, energy migration towards sites of high dissociation probability, and exciton dissociation during vibrational relaxation.

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