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Acquiring Permissible Load

2 Service Life for Technical Parts Under Mainly Static Loads 1.6.3.2.1 Acquiring Permissible Load [Pg.117]

As a rule, all technical components are dimensioned such that their expected service life is longer than the lifetime for which they are to be warranted. This is also true for each individual part, unless originally configured to be a wear part and characterized as such. All aspects of a particular load must be taken into consideration type, duration, temperature, media exposure, processing and post-processing operations. [Pg.117]

Despite the progress made in computer-aided treatment of structure-property relationships, dimensioning under such complex conditions continues to depend on experimental results obtained in creep investigations, S-N diagrams, as well as media and weathering investigations. [Pg.117]

ISO 9080 [114] describes a standard extrapolation method, abbreviated SEM, for predicting the service life creep behavior of pipes. The SEM method involves internal pressure tests at two or more temperatures, linear regression analysis with an estimation of regression quality, curve fitting and three different ways of expressing bend in hydrostatic pressure measurement. [Pg.118]

Left service iife determination under certain materia is and operating conditions (t = time, T = temperature, M = medium, P = processing)) [Pg.119]


Figure 8.2.15 One-dimensional spectra acquired with the four-coil probe. Each sample (250 mM in D2O) was loaded into the coil via the attached Teflon tubes 32 scans were acquired for each spectrum, with no delay between excitations of successive coils. Concurrent with the switch position being incremented, the spectral width was optimized for each compound 1 Hz line-broadening was applied before Fourier transformation and baseline correction. The spectral widths were (a) 600 Hz (galactose) (b) 1400 Hz (adenosine triphosphate) (c) 2000 Hz (chloroquine) (d) 500 Hz (fructose). 2048 complex data points were acquired for each spectrum, giving data acquisition times of approximately 1.7, 0.7, 0.5 and 2.0 s, respectively. The delay between successive 90 degree excitations was 4.9 s for each sample. Reprinted with permission From Li, Y., Walters, A., Malaway, P., Sweedler, J. V. and Webb, A. G., Anal. Chem.,l, 4815-4820 (1999). Copyright (1999) American Chemical Society... Figure 8.2.15 One-dimensional spectra acquired with the four-coil probe. Each sample (250 mM in D2O) was loaded into the coil via the attached Teflon tubes 32 scans were acquired for each spectrum, with no delay between excitations of successive coils. Concurrent with the switch position being incremented, the spectral width was optimized for each compound 1 Hz line-broadening was applied before Fourier transformation and baseline correction. The spectral widths were (a) 600 Hz (galactose) (b) 1400 Hz (adenosine triphosphate) (c) 2000 Hz (chloroquine) (d) 500 Hz (fructose). 2048 complex data points were acquired for each spectrum, giving data acquisition times of approximately 1.7, 0.7, 0.5 and 2.0 s, respectively. The delay between successive 90 degree excitations was 4.9 s for each sample. Reprinted with permission From Li, Y., Walters, A., Malaway, P., Sweedler, J. V. and Webb, A. G., Anal. Chem.,l, 4815-4820 (1999). Copyright (1999) American Chemical Society...
Fig. 3.16 (a) Formation of parallel ridges on PS imaged by CM-AFM under a load of 30 nN. The slow scan axis (down scan) was disabled hence the vertical axis corresponds to time. Reproduced with permission from [41]. Copyright 1999. Elsevier, (b) Contact mode AFM height image acquired with minimized forces on a PS film scanned previously with high... [Pg.101]

Fig. 3.50 A 2.5 x 2.5 im2 AFM image of lambda DNA on APS-modified mica acquired in CM-AFM in Tris buffer. This image was collected in normal contact mode, with loading force of 1 nN, using a Park sharpened tip (cantilever force constant of 0.1 N/m). Reproduced with permission from [106]. Copyright 1996. American Chemical Society... Fig. 3.50 A 2.5 x 2.5 im2 AFM image of lambda DNA on APS-modified mica acquired in CM-AFM in Tris buffer. This image was collected in normal contact mode, with loading force of 1 nN, using a Park sharpened tip (cantilever force constant of 0.1 N/m). Reproduced with permission from [106]. Copyright 1996. American Chemical Society...
Fig. 3.83 CM-AFM height images (acquired at constant load of 1 nN in buffered solution) in 3D projection of porous membranes with PAA coating visualized at different pH. Reproduced with permission from [174], Copyright 1998. American Chemical Society... Fig. 3.83 CM-AFM height images (acquired at constant load of 1 nN in buffered solution) in 3D projection of porous membranes with PAA coating visualized at different pH. Reproduced with permission from [174], Copyright 1998. American Chemical Society...
Fig. 4.18 Top Histogram of friction forces acquired at a constant load of 42 nN for PS films subjected to UV-ozone for (a) Os, (b) 20s, and (c) 40s. Bottom Plots of friction force versus applied load data recorded for untreated and UVO-treated PS films. The vertical arrow denotes increasing treatment time. Reproduced with permission from [39]. Copyright 2000. American Chemical Society... Fig. 4.18 Top Histogram of friction forces acquired at a constant load of 42 nN for PS films subjected to UV-ozone for (a) Os, (b) 20s, and (c) 40s. Bottom Plots of friction force versus applied load data recorded for untreated and UVO-treated PS films. The vertical arrow denotes increasing treatment time. Reproduced with permission from [39]. Copyright 2000. American Chemical Society...
Fig. 19 Experimental example of ultra-high resolution multidimensional NMR spectra obtained by the proposed technique 174 intra-residual resonance from 89 h 4D HNCACO- H -coupled experiment acquired for 5-79 fragment of bovine Ca -loaded Calbindin protein. Depicted cross-sections of 4D cube 50 x 450 x 40 x 100 Hz surrounding the peak allow determination of coupling constants from resolved 4D E.COSY pattern. JcaHa = 135.9 Hz, Jhnhci = 5.8 Hz, = —5.0 Hz, Jnhhcx = —10 Hz with numerical resolution of 0.4 Hz/point, 1.7 Hz/point, 0.2 Hz/point, and 0.7 Hz/point in dimensions F], F2, F3, and F4, respectively. Reprinted with permission from [80]... Fig. 19 Experimental example of ultra-high resolution multidimensional NMR spectra obtained by the proposed technique 174 intra-residual resonance from 89 h 4D HNCACO- H -coupled experiment acquired for 5-79 fragment of bovine Ca -loaded Calbindin protein. Depicted cross-sections of 4D cube 50 x 450 x 40 x 100 Hz surrounding the peak allow determination of coupling constants from resolved 4D E.COSY pattern. JcaHa = 135.9 Hz, Jhnhci = 5.8 Hz, = —5.0 Hz, Jnhhcx = —10 Hz with numerical resolution of 0.4 Hz/point, 1.7 Hz/point, 0.2 Hz/point, and 0.7 Hz/point in dimensions F], F2, F3, and F4, respectively. Reprinted with permission from [80]...

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