Optimum design of reinforced concrete retaining walls with the flower pollination algorithm

The flower pollination algorithm (FPA) is anefficient metaheuristicoptimizationalgorithm mimickingthe pollinationprocessof flowering species. In this study, FPA is applied, for first time, to the optimum design of reinforced concrete (RC) cantilever retaining walls. It is foundthat FPA offers important savings with respect to conventional design approachesand that it outperformsgenetic algorithm (GA)andthe particle swarm optimization (PSO) algorithm in this designproblem.Furthermore, parameter tuning reveals that the best FPA performance is achieved for switch probability values ranging between 0.4 and 0.7, a population size of 20 individualsand aLévy flightstep sizescale factor of 0.5. Finally, parametric optimum designs show that theoptimumcost of RC retaining walls increases rapidly with the wallheight and smoothly with the magnitude of surcharge loadin

Optimization and sensitivity of retaining structures

This paper is concerned with optimum design and sensitivity of retaining structures. The optimum design formulation in terms of a constrained nonlinear programming problem, is given for reinforced concrete-cantilever retaining walls. The objective function may be chosen as the cost or weight of the wall. The solution is carried out by a specially prepared computer program (RETOPT). Illustrative problems are solved, and their results are presented and discussed. The formulation allows for a detailed sensitivity analysis to be made for selected design parameters, also depicted with numerical examples

Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein

International audienceAgnoprotein is an important regulatory protein of the human polyoma JC virus (JCV) and plays critical roles during the viral replication cycle. It forms highly stable dimers and oligomers through its Leu/Ile/Phe-rich domain, which is important for the stability and function of the protein. We recently resolved the partial 3D structure of this protein by NMR using a synthetic peptide encompassing amino acids Thr17 to Gln52, where the Leu/Ile/Phe- rich region was found to adopt a major alpha-helix conformation spanning amino acids 23-39. Here, we report the resolution of the 3D structure of full-length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major α-helix domain at the same position but also revealed the presence of an additional minor α-helix region spanning amino acid residues Leu6 to lys13. The remaining regions of the protein adopt an intrinsically unstructured conformation. J. Cell. Biochem. 118: 3268-3280, 2017. © 2017 Wiley Periodicals, Inc