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These phenomena are interpreted by the perspective of fragility, molecular packing efficiency and intermolecular coupling.
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This is determined by the strength of a crystal lattice, which in turn is controlled primarily by four factors: the nature and number of intermolecular forces, molecular symmetry and packing efficiency, and the conformational degrees of freedom of a molecule [ 19].
The results are interpreted as a decrease of the efficiency of molecular packing with increasing network rigidity.
The success is based on the hyper-efficient molecular packing of the glucose.
We refer to this type of 2D IM-MS projection as conformational space analysis, as the differential scaling of mass (m/ z) and size (CCS) between molecular classes is indicative of differences in gas-phase packing efficiency.
Furthermore, measured densities and melting points, indicated differences in molecular packing for odd and even chain length compounds, attributed to geometries necessary for higher packing efficiencies and greater lattice stability.
Our analysis of 3413 protein structures having from 51 to 350 residues revealed that packing efficiency, indeed, is the same for proteins from different structural classes evidenced by the molecular volume per atom (for all-α proteins – 18.520±0.010 Å3, for all-β proteins −18.577±0.009 Å3, for α/β proteins −18.618±0.007 Å3, and for α+β proteins −18.598±0.009 Å3).
The hexagonal pyramid design had excellent stability and packing efficiency.
The crystal structures were obtained by molecular packing calculations.
C60/Ag(1 0 0) presents a unique uniaxially incommensurate molecular packing.
The mechanism probably encompasses restricted rotation and favorable molecular packing.
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