The weakly bound complex CO–orthoD2: Detection of millimeter-wave transitions

2000 ◽  
Vol 113 (20) ◽  
pp. 9351-9352 ◽  
Author(s):  
Leonid A. Surin ◽  
Boris S. Dumesh ◽  
Gisbert Winnewisser ◽  
Igor Pak
Keyword(s):  
Millimeter Wave ◽  
Weakly Bound

Millimeter-wave spectroscopy of weakly bound molecular complexes: Isotopologues of He-CO

2009 ◽  
Vol 106 (2) ◽  
pp. 183-189 ◽  
Author(s):  
A. V. Potapov ◽  
L. A. Surin ◽  
V. A. Panfilov ◽  
B. S. Dumesh
Keyword(s):  
Millimeter Wave ◽  
Molecular Complexes ◽  
Weakly Bound ◽  
Millimeter Wave Spectroscopy

A new millimeter-wave observation of the weakly bound CO–N 2 complex

2015 ◽  
Vol 307 ◽  
pp. 54-58 ◽  
Author(s):  
L.A. Surin ◽  
A. Potapov ◽  
H.S.P. Müller ◽  
S. Schlemmer
Keyword(s):  
Millimeter Wave ◽  
Weakly Bound ◽  
Wave Observation

scholarly journals Erratum: “Detection of the millimeter wave spectra of the weakly bound complexes 3He–CO and 4He–CO” [J. Chem. Phys. 112, 4064 (2000)]

2000 ◽  
Vol 112 (20) ◽  
pp. 9190-9190 ◽  
Author(s):  
Leonid A. Surin ◽  
Daniel A. Roth ◽  
Igor Pak ◽  
Boris S. Dumesh ◽  
Frank Lewen ◽  
...  
Keyword(s):  
Millimeter Wave ◽  
Chem Phys ◽  
Wave Spectra ◽  
Weakly Bound ◽  
Weakly Bound Complexes

Millimeter Wave Spectrum of the Weakly Bound Complex CH2═CHCN·H2O: Structure, Dynamics, and Implications for Astronomical Search

2015 ◽  
Vol 119 (48) ◽  
pp. 11674-11682 ◽  
Author(s):  
Camilla Calabrese ◽  
Annalisa Vigorito ◽  
Assimo Maris ◽  
Sergio Mariotti ◽  
Pantea Fathi ◽  
...  
Keyword(s):  
Millimeter Wave ◽  
Wave Spectrum ◽  
Weakly Bound ◽  
Structure Dynamics

Detection of the millimeter wave spectra of the weakly bound complexes 3He–CO and 4He–CO

2000 ◽  
Vol 112 (9) ◽  
pp. 4064-4068 ◽  
Author(s):  
Leonid A. Surin ◽  
Daniel A. Roth ◽  
Igor Pak ◽  
Boris S. Dumesh ◽  
Frank Lewen ◽  
...  
Keyword(s):  
Millimeter Wave ◽  
Wave Spectra ◽  
Weakly Bound ◽  
Weakly Bound Complexes

Millimeter-wave spectroscopy of the weakly bound molecular complex NH3-N2

2012 ◽  
Vol 113 (1) ◽  
pp. 1-4 ◽  
Author(s):  
A. V. Potapov ◽  
A. A. Dolgov ◽  
L. A. Surin
Keyword(s):  
Millimeter Wave ◽  
Molecular Complex ◽  
Weakly Bound ◽  
Millimeter Wave Spectroscopy

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.

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