Extended Ginzburg-Landau formalism: systematic expansion in small deviation from the critical temperature

Based on the Gor'kov formalism for a clean s-wave superconductor, we develop an extended version of the single-band Ginzburg-Landau (GL) theory by means of a systematic expansion in the deviation from the critical temperature T_c, i.e., tau=1-T/T_c. We calculate different contributions to the order parameter and the magnetic field: the leading contributions (~ tau^1/2 in the order parameter and ~ tau in the magnetic field) are controlled by the standard Ginzburg-Landau (GL) theory, while the next-to-leading terms (~ tau^3/2 in the gap and ~ tau^2 in the magnetic field) constitute the extended GL (EGL) approach. We derive the free-energy functional for the extended formalism and the corresponding expression for the current density. To illustrate the usefulness of our formalism, we calculate, in a semi-analytical form, the temperature-dependent correction to the GL parameter at which the surface energy becomes zero, and analytically, the temperature dependence of the thermodynamic critical field. We demonstrate that the EGL formalism is not just a mathematical extension to the theory - variations of both the gap and the thermodynamic critical field with temperature calculated within the EGL theory are found in very good agreement with the full BCS results down to low temperatures, which dramatically improves the applicability of the formalism compared to its standard predecessor

SPEXOR passive spinal exoskeleton decreases metabolic cost during symmetric repetitive lifting

PURPOSE: Besides mechanical loading of the back, physiological strain is an important risk factor for low-back pain. Recently a passive exoskeleton (SPEXOR) has been developed to reduce loading on the low back. We aimed to assess the effect of this device on metabolic cost of repetitive lifting. To explain potential effects, we assessed kinematics, mechanical joint work, and back muscle activity. METHODS: We recruited ten male employees, working in the luggage handling department of an airline company and having ample experience with lifting tasks at work. Metabolic cost, kinematics, mechanical joint work and muscle activity were measured during a 5-min repetitive lifting task. Participants had to lift and lower a box of 10 kg from ankle height with and without the exoskeleton. RESULTS: Metabolic cost was significantly reduced by 18% when wearing the exoskeleton. Kinematics did not change significantly, while muscle activity decreased by up to 16%. The exoskeleton took over 18-25% of joint work at the hip and L5S1 joints. However, due to large variation in individual responses, we did not find a significant reduction of joint work around the individual joints. CONCLUSION: Wearing the SPEXOR exoskeleton decreased metabolic cost and might, therefore, reduce fatigue development and contribute to prevention of low-back pain during repetitive lifting tasks. Reduced metabolic cost can be explained by the exoskeleton substituting part of muscle work at the hip and L5S1 joints and consequently decreasing required back muscle activity

Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein

Bacterial cell walls contain peptidoglycan, an essential polymer made by enzymes in the Mur pathway. These proteins are specific to bacteria, which make them targets for drug discovery. MurC, MurD, MurE and MurF catalyze the synthesis of the peptidoglycan precursor UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine by the sequential addition of amino acids onto UDP-N-acetylmuramic acid (UDP-MurNAc). MurC-F enzymes have been extensively studied by biochemistry and X-ray crystallography. In Gram-negative bacteria, ∼30–60% of the bacterial cell wall is recycled during each generation. Part of this recycling process involves the murein peptide ligase (Mpl), which attaches the breakdown product, the tripeptide L-alanyl-γ-D-glutamyl-meso-diaminopimelate, to UDP-MurNAc. We present the crystal structure at 1.65 Å resolution of a full-length Mpl from the permafrost bacterium Psychrobacter arcticus 273-4 (PaMpl). Although the Mpl structure has similarities to Mur enzymes, it has unique sequence and structure features that are likely related to its role in cell wall recycling, a function that differentiates it from the MurC-F enzymes. We have analyzed the sequence-structure relationships that are unique to Mpl proteins and compared them to MurC-F ligases. We have also characterized the biochemical properties of this enzyme (optimal temperature, pH and magnesium binding profiles and kinetic parameters). Although the structure does not contain any bound substrates, we have identified ∼30 residues that are likely to be important for recognition of the tripeptide and UDP-MurNAc substrates, as well as features that are unique to Psychrobacter Mpl proteins. These results provide the basis for future mutational studies for more extensive function characterization of the Mpl sequence-structure relationships