Microwave spectra, structure, and dynamics of the weakly bound complex, N2 CO2

2010 ◽  
Vol 133 (24) ◽  
pp. 244303 ◽  
Author(s):  
Daniel J. Frohman ◽  
Edwin S. Contreras ◽  
Ross S. Firestone ◽  
Stewart E. Novick ◽  
William Klemperer
Keyword(s):  
Weakly Bound ◽  
Structure And Dynamics ◽  
Microwave Spectra

Microwave spectra and structure of hydrogen cyanide-boron trifluoride: an almost weakly bound complex

1993 ◽  
Vol 97 (41) ◽  
pp. 10630-10637 ◽  
Author(s):  
S. W. Reeve ◽  
W. A. Burns ◽  
F. J. Lovas ◽  
R. D. Suenram ◽  
K. R. Leopold
Keyword(s):  
Hydrogen Cyanide ◽  
Boron Trifluoride ◽  
Weakly Bound ◽  
Microwave Spectra

Molecular Clusters:  Structure and Dynamics of Weakly Bound Systems

1996 ◽  
Vol 100 (31) ◽  
pp. 12945-12959 ◽  
Author(s):  
Zlatko Bačić ◽  
Roger E. Miller
Keyword(s):  
Molecular Clusters ◽  
Weakly Bound ◽  
Structure And Dynamics

scholarly journals Microwave spectra andab initiostudies of Ar-propane and Ne-propane complexes: Structure and dynamics

2007 ◽  
Vol 127 (18) ◽  
pp. 184306 ◽  
Author(s):  
Karen I. Peterson ◽  
David Pullman ◽  
Wei Lin ◽  
Andrea J. Minei ◽  
Stewart E. Novick
Keyword(s):  
Structure And Dynamics ◽  
Microwave Spectra

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.

Nucleosome dynamics

2006 ◽  
Vol 73 ◽  
pp. 109-119 ◽  
Author(s):  
Chris Stockdale ◽  
Michael Bruno ◽  
Helder Ferreira ◽  
Elisa Garcia-Wilson ◽  
Nicola Wiechens ◽  
...  
Keyword(s):  
High Resolution ◽  
Chromatin Structure ◽  
Current Knowledge ◽  
Dynamic Properties ◽  
Structure And Dynamics ◽  
Nucleosome Dynamics ◽  
Sharp Focus ◽  
Recent Advances ◽  
Insight Into ◽  
Chromatin Structure And Dynamics

In the 30 years since the discovery of the nucleosome, our picture of it has come into sharp focus. The recent high-resolution structures have provided a wealth of insight into the function of the nucleosome, but they are inherently static. Our current knowledge of how nucleosomes can be reconfigured dynamically is at a much earlier stage. Here, recent advances in the understanding of chromatin structure and dynamics are highlighted. The ways in which different modes of nucleosome reconfiguration are likely to influence each other are discussed, and some of the factors likely to regulate the dynamic properties of nucleosomes are considered.

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