It uses the generalized Dirac equation in the form [-ca vector.(p vector - gA vector/c)+E-V-βmc 2 +(μsub(a)/c)β(σ vector.cB vector-iα vector.E vector] PSI = 0, where α vector and β are the Dirac matrices, c is the velocity of light in vacuum, p vector equals i(h/2π)nabla vector is the pulse operator, g is the nuclear charge, A vector is the nuclear vector potential, E is the total energy of the nucleon, V is its nuclear potential energy, m is its rest mass, μsub(a) = -lambdasub(a)g(h/2π)/2m is the value of the anomalous nuclodynamic dipole moment, σ vector is the Pauli matrix, B vector = rot A vector/c is the nucleodynamic field intensity, i is the imaginary unity, E = -grad V/g is the nucleostatic field intensity, PSI is the Dirac wave function and (h/2π) is the Dirac action constant. For a nucleon in rest the potentials at distance r are V 0 = -(g 2 /4π)[esup(-μr)/r+μEi(-μr)], A vector 0 =(lambda sub(a)-1) (g(h/2π)/2mc) (esup(-μr)/4πr 3 ) (σ vector xr vector) with μ=0,684 fm -1 , αsub(g)=g 2 /4π(h/2π)c=1/4, lambda sub(a)=15.96 = 16 - αsub(g)/2π.αsub(g)/2π is the first order radiation correction, while 16 corresponds to a nuclear analogue of the Dirac magnetic monopole gsub(d) = 16 g = n4π(h/2π)c/2g for n = 8. These values are confirmed by calculations. In the Schroedinger equation approach it explains the spin-spin, tensor and spin-orbit forces, the velocity, energy and state dependence of the nuclear forces, the hard potential core, the ''many-body'' nuclear forces and fine effects of the nuclear interactions. (A.K.)
Õunpuu, Sylvia; Solomito, Matthew; Bell, Katharine; Pierz, Kristan
External femoral derotation osteotomy (FDO) is an orthopaedic intervention to correct increased femoral anteversion and associated excessive internal hip rotation and internal foot progression during gait in children with cerebral palsy. The resulting functional issues may include clearance problems and hip abductor lever-arm dysfunction. The purpose of this study was to evaluate long-term gait outcomes of FDO. Twenty ambulatory patients (27 sides) with cerebral palsy who underwent pre-operative (P0) and a one year post-operative (P1) gait analysis as part of the standard of care had a second post-operative analysis (P2) approximately 11 years post-surgical intervention. Mean hip rotation in stance showed statistically significant decreases in internal rotation at P1 post-surgical intervention that were maintained long-term (mean hip rotation P0: 21±9, P1: 0±9 and P2: 6±12 degrees internal). Similar results were seen with mean foot progression (P0: 9±16 degrees internal, P1: 14±13 degrees external, P2: 13±16 degrees external). However, 2/27 sides (9%) showed a recurrence of internal hip rotation of >15° at the 11year follow-up. The reasons for this recurrence could include age, surgical location and ongoing disease process all of which need to be further examined. We conclude that FDO can show long-term kinematic and functional benefits when performed in the prepubescent child with cerebral palsy in comparison to the natural progression of of hip rotation in cerebral palsy. Copyright © 2017 Elsevier B.V. All rights reserved.
Candel, Adela M; van Nuland, Nico A J; Martin-Sierra, Francisco M; Martinez, Jose C; Conejero-Lara, Francisco
A complete understanding of the thermodynamic determinants of binding between SH3 domains and proline-rich peptides is crucial to the development of rational strategies for designing ligands for these important domains. Recently we engineered a single-chain chimeric protein by fusing the alpha-spectrin Src homology region 3 (SH3) domain to the decapeptide APSYSPPPPP (p41). This chimera mimics the structural and energetic features of the interaction between SH3 domains and proline-rich peptides. Here we show that analysing the unfolding thermodynamics of single-point mutants of this chimeric fusion protein constitutes a very useful approach to deciphering the thermodynamics of SH3-ligand interactions. To this end, we investigated the contribution of each proline residue of the ligand sequence to the SH3-peptide interaction by producing six single Pro-Ala mutants of the chimeric protein and analysing their unfolding thermodynamics by differential scanning calorimetry (DSC). Structural analyses of the mutant chimeras by circular dichroism, fluorescence and NMR together with NMR-relaxation measurements indicate conformational flexibility at the binding interface, which is strongly affected by the different Pro-Ala mutations. An analysis of the DSC thermograms on the basis of a three-state unfolding model has allowed us to distinguish and separate the thermodynamic magnitudes of the interaction at the binding interface. The model assumes equilibrium between the "unbound" and "bound" states at the SH3-peptide binding interface. The resulting thermodynamic magnitudes classify the different proline residues according to their importance in the interaction as P2 approximately P7 approximately P10>P9 approximately P6>P8, which agrees well with Lim's model for the interaction between SH3 domains and proline-rich peptides. In addition, the thermodynamic signature of the interaction is the same as that usually found for this type of binding, with a strong enthalpy