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  • Lactobacillus delbrueckii subsp. lactis  (1)
  • Monte Carlo simulation  (1)
  • Life and Medical Sciences
  • Chemistry
  • Springer  (2)
  • 1995-1999  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Mathematical methods of operations research 46 (1997), S. 287-307 
    ISSN: 1432-5217
    Keywords: Reliability-based optimization ; structural reliability ; cost function ; nonlinear programming ; Monte Carlo simulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics , Economics
    Notes: Abstract A method to carry out a Reliability-Based Optimization (RBO) of especially nonlinear structural systems is introduced. Statistical uncertainties involving both structural and loading properties are considered. The concept is based on the separation of structural reliability analyses and the optimization procedures. Two approaches are discussed, depending on the interaction of reliability analysis and mathematical programming and the way of representation of the limit state functions (LSF) of the structure. As, for cases of practical significance, the LSF is known only pointwise it is approximated by Response Surfaces (RS). For the response calculations Finite Element (FE) procedures are utilized. Failure probabilities are determined by applying variance reducing Monte Carlo simulation (MCS) techniques such as Importance Sampling (IS). Following the reliability analysis, the optimization procedure is controlled by the NLPQL algorithm. A numerical example in terms of a template ocean platform exemplifies the procedures.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Prolidase ; Metalloprotease ; Lactobacillus delbrueckii subsp. lactis ; Nucleotide sequence analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From a genomic library of Lactobacillus delbrueckii subsp. lactis (DSM7290) DNA, in the low-copy-number vector pLG339, a recombinant clone was selected, which complemented a mutation in the prolidase gene (pepQ) of Escherichia coli UK173. Nucleotide sequence analysis revealed an open reading frame of 1104 nucleotides corresponding to a protein of 368 amino acids with a calculated pI of 4.64 and a molecular mass of 41087 Da. The start site of pepQ transcription was determined by primer extension analysis with mRNA prepared from L. delbrueckii. Based on homology of the gene product to various peptidases and on the substrate specificity determined, the peptidase was designated PepQ. The influence of various protease inhibitors and cations on peptidase activity indicated that PepQ is a metalloprotease. The absence of a membrane-spanning domain and a signal peptide sequence argues for a cytoplasmic localization of the enzyme.
    Type of Medium: Electronic Resource
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