The effect of phase fluctuations on the single-particle properties of the underdoped cuprates

We study the effect of order parameter phase fluctuations on the single-particle properties of fermions in the underdoped cuprate superconductors using a phenomenological low-energy theory. We identify the fermion-phase field coupling as the Doppler-shift of the quasiparticle spectrum induced by the fluctuating superfluid velocity and we calculate the effect of these fluctuations on the fermion self-energy. We show that the vortex pair unbinding near the superconducting transition causes a significant broadening in the fermion spectral function, producing a pseudogap-like feature. We also discuss the specific heat and show that the phase fluctuation effect is visible due to the short coherence length.Comment: RevTex 11 pages; 11 epsf figures included. Added and updated reference

Midgap edge states and pairing symmetry of quasi-one-dimensional organic superconductors

The singlet s-, d- and triplet p-wave pairing symmetries in quasi-one-dimensional organic superconductors can be experimentally discriminated by probing the Andreev bound states at the sample edges. These states have the energy in the middle of the superconducting gap and manifest themselves as a zero-bias peak in tunneling conductance into the corresponding edge. Their existence is related to the sign change of the pairing potential around the Fermi surface. We present an exact self-consistent solution of the edge problem showing the presence of the midgap states for p_x-wave superconductivity. The spins of the edge state respond paramagnetically to a magnetic field parallel to the vector d that characterizes triplet pairing.Comment: 6 pages, 4 figures. V.2: New section on spin response is added and references are updated. V.3: Final version accepted to PRB. Typos are corrected and important note is added in proof

Contraction-Induced Changes in Hydrogen Bonding of Muscle Hydration Water

Protein–water interaction plays a crucial role in protein dynamics and hence function. To study the chemical environment of water and proteins with high spatial resolution, synchrotron radiation-Fourier transform infrared (SR-FTIR) spectromicroscopy was used to probe skeletal muscle myofibrils. Observing the OH stretch band showed that water inside of relaxed myofibrils is extensively hydrogen-bonded with little or no free OH. In higher-resolution measurements obtained with single isolated myofibrils, the water absorption peaks were relatively higher within the center region of the sarcomere compared to those in the I-band region, implying higher hydration capacity of thick filaments compared to the thin filaments. When specimens were activated, changes in the OH stretch band showed significant dehydrogen bonding of muscle water; this was indicated by increased absorption at ∼3480 cm^–1 compared to relaxed myofibrils. These contraction-induced changes in water were accompanied by splitting of the amide I (CO) peak, implying that muscle proteins transition from α-helix to β-sheet-rich structures. Hence, muscle contraction can be characterized by a loss of order in the muscle–protein complex, accompanied by a destructuring of hydration water. The findings shed fresh light on the molecular mechanism of muscle contraction and motor protein dynamics