902 resultados para Stability of MPC
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Mode of access: Internet.
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ASTIA document no. AD215 482.
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Reproduced from typewritten copy.
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"This report is based on research sponsored by the U.S. Navy through the Office of Naval Research, Contract Nonr-2653(00)"
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"The existence of this giant monopoly [Interessen gemeinschaft der deutschen teerfarbenfabriken] raises vital military and economic questions, which are ... 'The riddle of the Rhine'."--p. 14.
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Mode of access: Internet.
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Mode of access: Internet.
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The cyclotides constitute a recently discovered family of plant-derived peptides that have the unusual features of a head-to-tail cyclized backbone and a cystine knot core. These features are thought to contribute to their exceptional stability, as qualitatively observed during experiments aimed at sequencing and characterizing early members of the family. However, to date there has been no quantitative study of the thermal, chemical, or enzymatic stability of the cyclotides. In this study, we demonstrate the stability of the prototypic cyclotide kalata B1 to the chaotropic agents 6 M guanidine hydrochloride (GdHCl) and 8 M urea, to temperatures approaching boiling, to acid, and following incubation with a range of proteases, conditions under which most proteins readily unfold. NMR spectroscopy was used to demonstrate the thermal stability, while fluorescence and circular dichroism were used to monitor the chemical stability. Several variants of kalata B1 were also examined, including kalata 132, which has five amino acid substitutions from B1, two acyclic permutants in which the backbone was broken but the cystine knot was retained, and a two-disulfide bond mutant. Together, these allowed determinations of the relative roles of the cystine knot and the circular backbone on the stability of the cyclotides. Addition of a denaturant to kalata B1 or an acyclic permutant did not cause unfolding, but the two-disulfide derivative was less stable, despite having a similar three-dimensional structure. It appears that the cystine knot is more important than the circular backbone in the chemical stability of the cyclotides. Furthermore, the cystine knot of the cyclotides is more stable than those in similar-sized molecules, judging by a comparison with the conotoxin PVIIA. There was no evidence for enzymatic digestion of native kalata B1 as monitored by LC-MS, but the reduced form was susceptible to proteolysis by trypsin, endoproteinase Glu-C, and thermolysin. Fluorescence spectra of kalata B1 in the presence of dithiothreitol, a reducing agent, showed a marked increase in intensity thought to be due to removal of the quenching effect on the Trp residue by the neighboring Cys5-Cys17 disulfide bond. In general, the reduced peptides were significantly more susceptible to chemical or enzymatic breakdown than the oxidized species.
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sThe structure of a two-chain peptide formed by the treatment of the potent antimicrobial peptide microcin J25 (MccJ25) with thermolysin has been characterized by NMR spectroscopy and mass spectrometry. The native peptide is 21 amino acids in size and has the remarkable structural feature of a ring formed by linkage of the side chain of Glu8 to the N-terminus that is threaded by the C-terminal tail of the peptide. Thermolysin cleaves the peptide at the Phe10-Val11 amide bond, but the threading of the C-terminus through the N-terminal ring is so tight that the resultant two chains remain associated both in the solution and in the gas phases. The three-dimensional structure of the thermolysin-cleaved peptide derived using NMR spectroscopy and simulated annealing calculations has a well-defined core that comprises the N-terminal ring and the threading C-terminal tail. In contrast to the well-defined core, the newly formed termini at residues Phe10 and Val11 are disordered in solution. The C-terminal tail is associated to the ring both by hydrogen bonds stabilizing a short beta-sheet and by hydrophobic interactions. Moreover, unthreading of the tail through the ring is prevented by the bulky side chains of Phe19 and Tyr20, which flank the octapeptide ring. This noncovalent two-peptide complex that has a remarkable stability in solution and in highly denaturing conditions and that survives in the gas phase is the first example of such a two-chain peptide lacking disulfide or interchain covalent bonds.
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Objectives: The aim of this study was to investigate the temperature profile of home intravenous (iv) antibiotic reservoirs and the stability of 16 megaunits of benzylpenicillin sodium in 120 mL of sodium chloride 0.9% at constant and variable temperatures. Methods: A Tinytag computerized thermometer recorded temperatures every minute in the home iv antibiotic reservoir pouches of nine patients over a 24 h period. Similar bags containing benzylpenicillin sodium (16 megaunits) were maintained either at a constant 36degreesC, 26degreesC or 21-22degreesC or were worn in a pouch by five healthy volunteers for a 24 h period. Other bags were stored at 3-5degreesC for 10 days. The bags were sampled at timed intervals and benzylpenicillin concentrations assayed by HPLC. Results: Median temperatures recorded in the infusion bags worn by the nine patients were in the range 16.7-34.1degreesC. For infusion bags maintained at 36degreesC, 26degreesC and 21-22degreesC, the concentrations of benzylpenicillin dropped below 90% of the initial concentration at a mean time of 5 h 18 min, 12 h 54 min and 13 h 20 min, respectively, whereas for bags worn by the healthy volunteers the mean time for 10% loss of benzylpenicillin was 9 h 20 min. In contrast, at 3-5degreesC, concentrations of benzylpenicillin only dropped below 90% of the initial concentration at 8 days. Conclusions: Significant temperature-dependent degradation of benzylpenicillin occurs during continuous home iv antibiotic programme infusions, which could result in loss of efficacy.
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In broader catchment scale investigations, there is a need to understand and ultimately exploit the spatial variation of agricultural crops for an improved economic return. In many instances, this spatial variation is temporally unstable and may be different for various crop attributes and crop species. In the Australian sugar industry, the opportunity arose to evaluate the performance of 231 farms in the Tully Mill area in far north Queensland using production information on cane yield (t/ha) and CCS ( a fresh weight measure of sucrose content in the cane) accumulated over a 12-year period. Such an arrangement of data can be expressed as a 3-way array where a farm x attribute x year matrix can be evaluated and interactions considered. Two multivariate techniques, the 3-way mixture method of clustering and the 3-mode principal component analysis, were employed to identify meaningful relationships between farms that performed similarly for both cane yield and CCS. In this context, farm has a spatial component and the aim of this analysis was to determine if systematic patterns in farm performance expressed by cane yield and CCS persisted over time. There was no spatial relationship between cane yield and CCS. However, the analysis revealed that the relationship between farms was remarkably stable from one year to the next for both attributes and there was some spatial aggregation of farm performance in parts of the mill area. This finding is important, since temporally consistent spatial variation may be exploited to improve regional production. Alternatively, the putative causes of the spatial variation may be explored to enhance the understanding of sugarcane production in the wet tropics of Australia.
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This paper re-examines the stability of multi-input multi-output (MIMO) control systems designed using sequential MIMO quantitative feedback theory (QFT). In order to establish the results, recursive design equations for the SISO equivalent plants employed in a sequential MIMO QFT design are established. The equations apply to sequential MIMO QFT designs in both the direct plant domain, which employs the elements of plant in the design, and the inverse plant domain, which employs the elements of the plant inverse in the design. Stability theorems that employ necessary and sufficient conditions for robust closed-loop internal stability are developed for sequential MIMO QFT designs in both domains. The theorems and design equations facilitate less conservative designs and improved design transparency.