3,266 research outputs found

    The Nationalism of Swift v. Tyson

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    An ellipsometric study of protein adsorption at the saliva-air interface

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    At the liquid-air interface of human saliva a protein layer is adsorbed. From ellipsometric measurements it was found that the thickness of the surface layer ranged from 400 to 3600 Å and the amount of protein material adsorbed was 9–340 mg/m2. Based on the concentration of protein in the layer the samples could be classified into two groups: a low concentration (ca. 0.15 g/ml) and a high concentration (0.7–1.1 g/ml). In the low concentration group the surface layers appeared to be thin (500–600 Å) while those in the high concentration group appeared to be much thicker (1000–3500 Å). A correlation between the bulk pH and the thickness of the surface layer could be established

    Rheological properties of human saliva

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    From measurements with a Couette-type viscometer provided with a guard ring it was shown that at the saliva-air interface a protein layer is adsorbed. Measurements of the surface shear modulus of this layer on saliva of 7 healthy subjects were performed at a frequency of about 70 Hz and a temperature of 25 °C. For a surface age of about 1.5 h the surface shear modulus and the surface viscosity were in the order of 1 Nm−1 and 10−3 Nm−1 s, respectively. From ellipsometric measurements it was found that the thickness of the protein layer was approx. 100nm and, using this value, it could be concluded that the shear modulus and the dynamic viscosity were in the order of 107 Pa and 104 Pa s, respectively. The layer appeared to be fragile. Even shear deformation amplitudes of 4 × 10−5 are too high to assure linearity. The complex viscosity (η = η′ − iη′′) of the bulk liquid of human submandibular saliva below the absorbed layer was measured in the frequency range 70 Hz–200 kHz with 3 torsional resonators, each for a different frequency, and a Ni-tube resonator. It was concluded, that the real part of the complex viscosity (η′) decreases from 1.1 mPa s at 70 Hz to a value of 0.95 mPa s at high frequencies. Except at the lowest frequency (70 Hz), the value of η′′ was too small to be detected

    A New Simulated Annealing Algorithm for the Multiple Sequence Alignment Problem: The approach of Polymers in a Random Media

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    We proposed a probabilistic algorithm to solve the Multiple Sequence Alignment problem. The algorithm is a Simulated Annealing (SA) that exploits the representation of the Multiple Alignment between DD sequences as a directed polymer in DD dimensions. Within this representation we can easily track the evolution in the configuration space of the alignment through local moves of low computational cost. At variance with other probabilistic algorithms proposed to solve this problem, our approach allows for the creation and deletion of gaps without extra computational cost. The algorithm was tested aligning proteins from the kinases family. When D=3 the results are consistent with those obtained using a complete algorithm. For D>3D>3 where the complete algorithm fails, we show that our algorithm still converges to reasonable alignments. Moreover, we study the space of solutions obtained and show that depending on the number of sequences aligned the solutions are organized in different ways, suggesting a possible source of errors for progressive algorithms.Comment: 7 pages and 11 figure

    Sequence Alignment with Matched Sections

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    In molecular biology, two finite sequences are compared by displaying one sequence written over another in an alignment. The number of alignments of two sequences is related to the Stanton-Cowan numbers. This paper gives asymptotics for the number of alignments of two sequences of length n with matching sections of size at least b
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