ClF2: Structure and infrared spectra of a weakly bound triatomic molecule

1993 ◽  
Vol 98 (10) ◽  
pp. 8051-8056 ◽  
Author(s):  
John Morrison Galbraith ◽  
George Vacek ◽  
Henry F. Schaefer
Keyword(s):  
Infrared Spectra ◽  
Triatomic Molecule ◽  
Weakly Bound

ChemInform Abstract: ClF2: Structure and Infrared Spectra of a Weakly Bound Triatomic Molecule.

ChemInform ◽  
2010 ◽  
Vol 24 (36) ◽  
pp. no-no
Author(s):  
J. M. GALBRAITH ◽  
G. VACEK ◽  
H. F. III SCHAEFER
Keyword(s):  
Infrared Spectra ◽  
Triatomic Molecule ◽  
Weakly Bound

Infrared spectra of carbocations and CH4+ in helium

2021 ◽  
Author(s):  
Julia Ann Davies ◽  
Shengfu Yang ◽  
Andrew M Ellis
Keyword(s):  
Ir Spectra ◽  
Infrared Spectra ◽  
Electron Ionization ◽  
Weakly Bound ◽  
Cation Complexes

Infrared (IR) spectra of several hydrocarbon cations are reported, namely CH3+, CH4+, CH5+, CH5+(CH4) and C2H5+. The spectra were generated from weakly-bound helium-cation complexes formed by electron ionization of helium...

scholarly journals Micro-solvation of CO in water: infrared spectra and structural calculations for (D2O)2–CO and (D2O)3–CO

2019 ◽  
Vol 21 (48) ◽  
pp. 26564-26568
Author(s):  
A. J. Barclay ◽  
A. Pietropolli Charmet ◽  
K. H. Michaelian ◽  
A. R. W. McKellar ◽  
N. Moazzen-Ahmadi
Keyword(s):  
Infrared Spectra ◽  
Molecular Clusters ◽  
Fundamental Region ◽  
Weakly Bound

The weakly-bound molecular clusters (D2O)2–CO and (D2O)3–CO are observed in the C–O stretch fundamental region (≈2150 cm−1), and their rotationally-resolved infrared spectra yield precise rotational parameters.

Infrared Spectroscopy of Solvation and Isomers in Fe+(H2O)1,2Arm Complexes

2004 ◽  
Vol 57 (12) ◽  
pp. 1145 ◽  
Author(s):  
Richard S. Walters ◽  
Michael A. Duncan
Keyword(s):  
Infrared Spectroscopy ◽  
Infrared Spectra ◽  
Metal Cation ◽  
Pure Metal ◽  
Laser Vaporization ◽  
Weakly Bound ◽  
A Minor ◽  
Ion Molecule Complexes ◽  
Asymmetric Stretch ◽  
Pulsed Nozzle

Vibrational spectroscopy in the OH-stretching region is reported for the mass-selected ion–molecule complexes Fe+(H2O)Ar2 and Fe+(H2O)2Ar. These species are produced by laser vaporization in a pulsed nozzle cluster source, mass-selected with a reflectron time-of-flight mass spectrometer, and studied with infrared laser photodissociation spectroscopy. To achieve efficient photodissociation, the pure metal–water complexes are ‘tagged’ with weakly bound argon atoms. Such tagging is expected to exert a minor perturbation on the spectroscopy. However, we find that this may not be true depending on the binding site. The symmetric stretch and asymmetric stretch of water in these complexes shifts 30–50 cm−1 to the red as a result of binding to the metal cation, and an additional redshift is found for isomers with argon bound to the OH of water. The relationships between isomers and infrared spectra are discussed.

The weakly bound complex CH4-H2: Observation and analysis of infrared spectra in the 350 and 1311 cm−1 regions

1999 ◽  
Vol 110 (20) ◽  
pp. 9989-9996 ◽  
Author(s):  
A. R. W. McKellar ◽  
D. A. Roth ◽  
I. Pak ◽  
G. Winnewisser
Keyword(s):  
Infrared Spectra ◽  
Weakly Bound

Structure, Energetics, and Infrared Spectra of Weakly Bound HC2n+1N···HCl Complexes. A Theoretical Study

2012 ◽  
Vol 116 (23) ◽  
pp. 5665-5673 ◽  
Author(s):  
Marcin Gronowski ◽  
Robert Kołos ◽  
Joanna Sadlej
Keyword(s):  
Infrared Spectra ◽  
Theoretical Study ◽  
Weakly Bound

Infrared spectra of acetonitrile sorbed on porous glass

1970 ◽  
Vol 48 (1) ◽  
pp. 7-12 ◽  
Author(s):  
M. J. D. Low ◽  
P. L. Bartner
Keyword(s):  
Infrared Spectra ◽  
Porous Glass ◽  
Weakly Bound ◽  
Surface Complexes ◽  
Surface Hydroxyls ◽  
Hydrogen Bonded

Infrared spectra were recorded of acetonitrile sorbed on highly degassed porous glass as well as on silica and B-, Al-, and Zr-impregnated porous glass and silica. Most of the acetonitrile was weakly and reversibly adsorbed, becoming hydrogen-bonded to surface hydroxyls. A small amount of the adsorbate formed weakly bound surface complexes with Al- and Zr-, but not with B-impurities.

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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