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At least 1,225 records · Page 68Linked to original sources
PubMed2003

The effect of dance training on joint mobility, muscle flexibility, speed and agility in young cross-country skiers--a prospective controlled intervention study.

We evaluated a short-term (3 months) and a long-term (8 months) effect of dance training on joint mobility and muscle flexibility of the spine, hip and ankle and on speed and agility in young cross-country skiers. Twenty elite cross-country skiers - aged 12-15 years - participated in the study. Five males and five females received dance training (intervention group) and five males and five females did not dance (reference group). Joint mobility and muscle flexibility of the spine, hip and ankle joints were measured using a goniometer, a kyphometer, a measuring tape and a ruler. Two sports-related functional tests - the slalom-test and the hurdle-test - were also performed. These measurements/tests were performed before the start of the dancing period and after 3 and 8 months. The subjects from the intervention group increased their speed with 0.3 s after 3 (P = 0.05) and 8 months (P = 0.02), respectively, when measured with the slalom-test. They also improved their speed and agility according to the hurdle-test after 3 months with 0.8 s (P = 0.000) and 8 months with 0.6 s (P = 0.01). Furthermore, they increased flexion-extension of the thoracic spine with 7.5 degrees after 3 months (P = 0.05) and with 9 degrees degrees after 8 months (P = 0.03) and lateral flexion of the spine with 0.04 m (P = 0.005) and 0.03 m (P = 0.02) after 3 and 8 months, respectively. The reference group was impaired or unchanged in the studied parameters after both 3 and 8 months. We conclude that dance training has a positive effect on speed and agility and on joint mobility and muscle flexibility in flexion-extension and lateral flexion of the spine in young cross-country skiers.

Adolescent↗
PubMed2000

Rationale for the use of low-torque endodontic motors in root canal instrumentation.

Fracture of nickel-titanium rotary files is an iatrogenic error which can seriously jeopardize root canal therapy. If a high-torque motor is used, the instrument-specific limit-torque (fracture limit) is often exceeded, thus increasing the risk of intracanal failure. A possible solution to this problem is to use a low-torque endodontic motor which operates below these values. If the torque is set just below the limit of elasticity for each instrument, the risk of fracture is likely to be markedly reduced. The purpose of this paper was to discuss mechanical properties of NiTi rotary instruments, the rationale for selecting low torque values, and to use clinically a new endodontic motor (step-motor) which operates below the limit of elasticity of each rotary file. The step-motor was found to be helpful in reducing the risk of instrument fracture. Irreversible material damage (plastic deformation) and instrument fracture were rarely seen. Low-torque instrumentation also increased tactile sense and, consequently, mental awareness of rotary instrumentation.

Computer Systems↗
PubMed1999

Crystal structure of human heme oxygenase-1.

Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme iron ligand, His 25. Conserved glycines in the distal helix near the oxygen binding site allow close contact between the helix backbone and heme in addition to providing flexibility for substrate binding and product release. Regioselective oxygenation of the alpha-meso heme carbon is due primarily to steric influence of the distal helix.

Binding Sites↗
PubMed1999

Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.

XRCC1 functions in the repair of single-strand DNA breaks in mammalian cells and forms a repair complex with beta-Pol, ligase III and PARP. Here we describe the NMR solution structure of the XRCC1 N-terminal domain (XRCC1 NTD). The structural core is a beta-sandwich with beta-strands connected by loops, three helices and two short two-stranded beta-sheets at each connection side. We show, for the first time, that the XRCC1 NTD specifically binds single-strand break DNA (gapped and nicked). We also show that the XRCC1 NTD binds a gapped DNA-beta-Pol complex. The DNA binding and beta-Pol binding surfaces were mapped by NMR and found to be well suited for interaction with single-strand gap DNA containing a 90 degrees bend, and for simultaneously making contacts with the palm-thumb of beta-Pol in a ternary complex. The findings suggest a mechanism for preferential binding of the XRCC1 NTD to flexible single-strand break DNA.

Amino Acid Sequence↗
PubMed1999

Tying a molecular knot with optical tweezers.

Filamentous structures are abundant in cells. Relatively rigid filaments, such as microtubules and actin, serve as intracellular scaffolds that support movement and force, and their mechanical properties are crucial to their function in the cell. Some aspects of the behaviour of DNA, meanwhile, depend critically on its flexibility-for example, DNA-binding proteins can induce sharp bends in the helix. The mechanical characterization of such filaments has generally been conducted without controlling the filament shape, by the observation of thermal motions or of the response to external forces or flows. Controlled buckling of a microtubule has been reported, but the analysis of the buckled shape was complicated. Here we report the continuous control of the radius of curvature of a molecular strand by tying a knot in it, using optical tweezers to manipulate the strand's ends. We find that actin filaments break at the knot when the knot diameter falls below 0.4 microm. The pulling force at breakage is around 1 pN, two orders of magnitude smaller than the tensile stress of a straight filament. The flexural rigidity of the filament remained unchanged down to this diameter. We have also knotted a single DNA molecule, opening up the possibility of studying curvature-dependent interactions with associated proteins. We find that the knotted DNA is stronger than actin.

Actins↗
PubMed1999

Dynamics of individual flexible polymers in a shear flow.

Polymer dynamics are of central importance in materials science, mechanical engineering, biology and medicine. The dynamics of macromolecular solutions and melts in shear flow are typically studied using bulk experimental methods such as light and neutron scattering and birefringence. But the effect of shear on the conformation and dynamics of individual polymers is still not well understood. Here we describe observations of the real-time dynamics of individual, flexible polymers (fluorescently labelled DNA molecules) under a shear flow. The sheared polymers exhibit many types of extended conformation with an overall orientation ranging from parallel to perpendicular with respect to the flow direction. For shear rates much smaller than the inverse of the relaxation time of the molecule, the relative populations of these two main types of conformation are controlled by the rate of the shear flow. These results question the adequacy of assumptions made in standard models of polymer dynamics.

Biopolymers↗
PubMed2004

Feeding mechanisms: Hummingbird jaw bends to aid insect capture.

The upper jaws of birds, unlike those in many tetrapods, move relative to the skull and are often flexible along their length, whereas the lower jaw (mandible) is usually a rigid structure formed by the fusion of several bones, flexing only where it meets the skull. Here we describe a previously unnoticed mandibular bending movement in hummingbirds, in which the distal half of the mandible is actively flexed downwards and the gape widens to catch flying insects. The hummingbird is thought to have developed a long narrow bill as it specialized in feeding on floral nectar, but the bird's need to supplement its diet with insects must have contributed to the surprising flexibility of its jaw.

Adaptation, Physiological↗
PubMed2004

On the move.

Explore the source record for details and available documents.

Catalysis↗
PubMed2000

Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex.

The response of the internal dynamics of calcium-saturated calmodulin to the formation of a complex with a peptide model of the calmodulin-binding domain of the smooth muscle myosin light chain kinase has been studied using NMR relaxation methods. The backbone of calmodulin is found to be unaffected by the binding of the domain, whereas the dynamics of side chains are significantly perturbed. The changes in dynamics are interpreted in terms of a heterogeneous partitioning between structure (enthalpy) and dynamics (entropy). These data provide a microscopic view of the residual entropy of a protein in two functional states and suggest extensive enthalpy/entropy exchange during the formation of a protein-protein interface.

Amino Acid Sequence↗