Comparison between structural and residual error formulations of an optimum design mechanism problem

Summary The model formulation of the objective function is one of the most important steps for solving an optimization problem. Generally, the objective function of an optimal design mechanism problem can be mathematically formulated either with structural or residual errors. In this paper we have conducted some comparisons between the results obtained by the structural and residual error formulations utilized in solving the optimum design of a four-bar linkage. The optimization problem is defined as a nonlinear least-squares problem. The damped Gauss-Newton algorithm is utilized for computing the solution, which ensures a local convergence for almost all nonlinear least-squares problems.

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Sommario La formulazione matematica della funzione obiettivo è uno degli aspetti più delicati nella soluzione di un problema di ottimizzazione. Generalmente la funzione obiettivo di un problema di progettazione ottima di un meccanismo può essere formulata sia mediante l'errore strutturale che residuo. In questo lavoro sono stati eseguiti dei confronti tra i risultati ottenuti mediante le due precedenti formulazioni, in riferimento al problema della progettazione ottima di un quadrilatero articolato. Il problema di ottimizzazione viene definito come un problema nonlineare ai minimi quadrati la cui soluzione numerica è ottenuta mediante l'algoritmo damped di Gauss-Newton.

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This paper was partially discussed at theII Congegno di Meccanica Computazionale, Roma, 1987.     

Rapid detection and identification of liquid crystal states by light scattering

Thermotropic mesophases can be detected by the light scattering properties of these phases. This article deals with a rapid scan technique for the detection and characterization of these mesophases by measuring light scattering as a function of temperature. From the number of compounds studied it is apparent that the method allows for a rapid and reasonably precise determination of transition temperatures. In addition, the method is found to be useful in the characterization of mesophases, in particular the nematic phase.     

Electrospray ionization quadrupole time-of-flight and matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometric analyses to solve micro-heterogeneity in post-translationally modified peptides from Phoneutria nigriventer (Aranea, Ctenidae) venom

Previous studies of the fractionated venom of the Brazilian armed spider Phoneutria nigriventer, obtained by gel filtration, have demonstrated the presence of a fraction PhM, a pool of small peptides (up to 2000 Da) that provoke contractions in smooth muscle of guinea pig ileum. Initial attempts to sequence these peptides were largely unsuccessful because of the low purification yield and the fact that the majority seemed to be blocked at their N-termini. In the present work, analysis of this venom fraction by mass spectrometry has revealed the existence of a highly complex mixture of peptides with molecular weights corresponding to those observed for the muscle-active peptides previously described (800-1800 Da). These peptides appear to be a family of isoforms with some particular features. The amino acid sequences of 15 isoforms have been determined by tandem mass spectrometry (MS/MS) using both electrospray ionization quadrupole time-of-flight mass spectrometry (ESI-Q/ToFMS) and matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry (MALDI-ToF/ToFMS). These molecules contain post-translational modifications such as proteolysis and C-terminal amidation, which combine to generate additional isoforms. All the isoforms sequenced in this study possess an N-terminal pyroglutamic acid residue. A search for sequence similarities with other peptides in databanks revealed that these peptides are structurally related to the tachykinins, a family of neuro-hormone peptides. The data obtained in this study will be essential for the subsequent steps of this research, the synthesis of these peptides and pharmacological characterization of their biological activity.     

Study of the microstructure of tetrahydrofuran-3,3 dimethyloxetane copolymers by 13C-NMR spectroscopy.

The microstructure of tetrahydrofuran (A)-3,3 dimethyloxetane (B) copolymers was studied by ¹³C-{¹H}-NMR spectroscopy. Only the methyl carbons corresponding to the 3,3 dimethyloxetane unit appear as a singlet, whereas the other carbons present a more complicated spectral pattern than it would be expected if ? effects were negligible. The assignment of the resonance signals allowed the determination of the values of the probabilities of the different triads, which were in good agreement with those obtained from the reactivity ratios.