W artykule przedstawiono algorytm projektowania przekrojów prostokątnych i teowych z uwzględnieniem paraboliczno-prostokątnego wykresu naprężeń w strefie ściskanej betonu. Rozpisano równania równowagi sił dla przekroju prostokątnego i teowego, wyznaczono bezwymiarowe funkcje parametrów geometrycznych, opracowano i podano tablice do praktycznego projektowania przekrojów według ustalonych algorytmów.
EN
An algorithm of rectangular and T -bar sections with respect to re'ctangular -parabola graph of stress in concrete concentration zone was presented in the article. Equilibrium of forces equation for rectangular and T -bar sections were written at length, dimensionless functions of geometrical parameters were calculated, tables for practical designing of sections according to established algorithms were worked out and stated.
Three peptides with sequences related to the binding loop of Cucurbita maxima trypsin inhibitor III were obtained: [G3,GIO]CMTI-HI (1-10) (1), [A1,G3,A9,G10]MTlII (1-10) (2) and c(K-A-A-P-R-I-L-M-K-Y-A-E) (3). All peptides were synthesized by the solid-phase methodusing the Fmoc/Bu t procedure. Peptide 1 revealed a relatively high inhibitory activity (association equilibrium constant with bovine beta-trypsin Ka = 4 x 10 9 [M -1]). Significantly lower activity (Ka = 3.6x l O4 [M -1) was obtained for peptide 3. Peptide 2 appeared to be inactive.
Two analogues of peptidic trypsin inhibitor isolated from seeds of Ecballium elaterium (EETI-II): [Pen19,21,27] EETI-II (1) and [Hcy19,21,27] EETI-II (2) were synthesized by the solid-phase method using the Fmoc/But procedure. Their inhibitory activity was determined by the calculation of association equilibrium constants (Ka) with bovine _-trypsin. In comparison with the parent compound, both analogues showed reduced trypsin inhibitory activity more than 7 and 18 times, respectively. We postulate that the observed differences may reflect the role of disulfide bridges in the interaction of inhibitors with trypsin or the introduced modifications change the conformational equilibrium of the analogues synthesized towards conformation(s) less favorable for the interaction with the enzyme.
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