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Though YB6 and LaB6 share the same crystal structure, atomic valence electron configuration, and phonon modes, they exhibit drastically different phonon-mediated superconductivity. YB6 superconducts below 8.4 K, giving it the second-highest critical temperature of known borides, second only to MgB2. LaB6 does not superconduct until near-absolute zero temperatures (below 0.45 K), however. Though previous studies have quantified the canonical superconductivity descriptors of YB6's greater Fermi-level (Ef ) density of states and higher electron-phonon coupling (EPC), the root of this difference has not been assessed with full detail of the electronic structure. Through chemical bonding, we determine low-lying, unoccupied 4f atomic orbitals in lanthanum to be the key difference between these superconductors. These orbitals, which are not accessible in YB6, hybridize with π B-B bonds and bring this π-system lower in energy than the σ B-B bonds otherwise at Ef. This inversion of bands is crucial: the optical phonon modes we show responsible for superconductivity cause the σ-orbitals of YB6 to change drastically in overlap, but couple weakly to the π-orbitals of LaB6. These phonons in YB6 even access a crossing of electronic states, indicating strong EPC. No such crossing in LaB6 is observed. Finally, a supercell (the M k-point) is shown to undergo Peierls-like effects in YB6, introducing additional EPC from both softened acoustic phonons and the same electron-coupled optical modes as in the unit cell. Overall, we find that LaB6 and YB6 have fundamentally different mechanisms of superconductivity, despite their otherwise near-identity. [ABSTRACT FROM AUTHOR]

Here we present a model to estimate the interaction free energy contribution of each amino acid residue of a given protein. Protein interaction energy is described in terms of per-residue interaction factors, μ. Multibody interactions are implicitly captured in μ through the combination of amino acid terms (γ) guided by local conformation indices (σ). The model enables construction of an interaction factor heat map for a protein in a given fold, allows prima facie assessment of the degree of residue–residue interaction, and facilitates a qualitative and quantitative evaluation of protein association properties. The model was used to compute thermal stability of T4 bacteriophage lysozyme mutants across seven sites. Qualitative assessment of mutational effects provides a straightforward rationale regarding whether a particular site primarily perturbs native or non-native states, or both. The presented model was found to be in good agreement with experimental mutational data ( R 2 = 0. 7 3) and suggests an approach by which to convert structure space into energy space. [ABSTRACT FROM AUTHOR]