• Title/Summary/Keyword: Nonregular design

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Classification Rule for Optimal Blocking for Nonregular Factorial Designs

  • Park, Dong-Kwon;Kim, Hyoung-Soon;Kang, Hee-Kyoung
    • Communications for Statistical Applications and Methods
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    • v.14 no.3
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    • pp.483-495
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    • 2007
  • In a general fractional factorial design, the n-levels of a factor are coded by the $n^{th}$ roots of the unity. Pistone and Rogantin (2007) gave a full generalization to mixed-level designs of the theory of the polynomial indicator function using this device. This article discusses the optimal blocking scheme for nonregular designs. According to hierarchical principle, the minimum aberration (MA) has been used as an important criterion for selecting blocked regular fractional factorial designs. MA criterion is mainly based on the defining contrast groups, which only exist for regular designs but not for nonregular designs. Recently, Cheng et al. (2004) adapted the generalized (G)-MA criterion discussed by Tang and Deng (1999) in studying $2^p$ optimal blocking scheme for nonregular factorial designs. The approach is based on the method of replacement by assigning $2^p$ blocks the distinct level combinations in the column with different blocks. However, when blocking level is not a power of two, we have no clue yet in any sense. As an example, suppose we experiment during 3 days for 12-run Plackett-Burman design. How can we arrange the 12-runs into the three blocks? To solve the problem, we apply G-MA criterion to nonregular mixed-level blocked scheme via the mixed-level indicator function and give an answer for the question.

A New Approach for Selecting Fractional Factorial Designs

  • Park, Dong-Kwon;Kim, Hyoung-Soon
    • Journal of the Korean Data and Information Science Society
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    • v.14 no.3
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    • pp.707-714
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    • 2003
  • Because of complex aliasing, nonregular designs have traditionally been used for screening only main effects. However, complex aliasing actually may allow some interactions entertained and estimated without making additional runs. According to hierarchical principle, the minimum aberration has been used as an important criterion for selecting regular fractional factorial designs. The criterion is not applicable to nonregular designs. In this paper, we give a criterion for choosing fractional factorial designs based on the fan theory. The criterion is focused on the partial ordering given by set inclusion on estimable sets which is called leaves.

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A Novel Strategy for Thermostability Improvement of Trypsin Based on N-Glycosylation within the Ω-Loop Region

  • Guo, Chao;Liu, Ye;Yu, Haoran;Du, Kun;Gan, Yiru;Huang, He
    • Journal of Microbiology and Biotechnology
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    • v.26 no.7
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    • pp.1163-1172
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    • 2016
  • The Ω-loop is a nonregular and flexible structure that plays an important role in molecular recognition, protein folding, and thermostability. In the present study, molecular dynamics simulation was carried out to assess the molecular stability and flexibility profile of the porcine trypsin structures. Two Ω-Loops (fragment 57-67 and fragment 78-91) were confirmed to represent the flexible region. Subsequently, glycosylation site-directed mutations (A73S, N84S, and R104S) were introduced within the Ω-loop region and its wing chain based on its potential N-glycosylation sites (Asn-Xaa-Ser/Thr consensus sequences) and structure information to improve the thermostability of trypsin. The result demonstrated that the half-life of the N84S mutant at 50℃ increased by 177.89 min when compared with that of the wild-type enzyme. Furthermore, the significant increase in the thermal stability of the N84S mutant has also been proven by an increase in the Tm values determined by circular dichroism. Additionally, the optimum temperatures of the wild-type enzyme and the N84S mutant were 75℃ and 80℃, respectively. In conclusion, we obtained the thermostability-improved enzyme N84S mutant, and the strategy used to design this mutant based on its structural information and N-linked glycosylation modification could be applied to engineer other enzymes to meet the needs of the biotechnological industry.