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一种预测木聚糖酶最适温度的PCANN模型 被引量:1

A Principal Component-Artificial Neural Network Model for Predicting Optimum Temperature in F/10 Xylanases
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摘要 采用主成分分析法对样本数据集进行预处理,将得到的新样本数据集输入神经网络,构建F/10家族木聚糖酶氨基酸组成和最适温度的主成分分析神经网络(PCANN)模型.结果表明,当学习速率为0.07、动态参数为0.8、Sigmoid参数为0.96,隐含层结点数为5时,模型对温度拟合的平均绝对百分比误差为4.97%,绝对误差为3.03℃.同时,方法具有良好的预测效果,预测的平均绝对百分比误差为4.68%,平均绝对误差为3.55℃. The principal component analysis was first applied to the data processing in training sets, and then the obtained new principal components were used as input parameters of BP neural networks. A prediction model for optimum temperature of xylanases in F/10 family was established based on uniform design. When the learning rate, momentum parameter, Sigmoid parameter and the neuron numbers of the hidden layer was 0. 07,0. 8,0. 96 and 5, respectively, the eaiculated temperatures fitted the reported optimum temperatures very well. The mean absolute percent error was 4. 97%. At the same time, the predicted temperatures fitted the reported optimum temperatures well and the mean absolute error was 3.55 ℃.It was superior in fittings and predictions compared to the reported model based on stepwise regression,
出处 《华侨大学学报(自然科学版)》 CAS 北大核心 2007年第1期55-58,共4页 Journal of Huaqiao University(Natural Science)
基金 国务院侨务办公室科研基金资助项目(05Q0018)
关键词 主成分分析 BP神经网络 木聚糖酶 最适温度 虚拟筛选 principal component analysis BP neural networks xylanase optimum temperature virtual screening
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参考文献9

  • 1ANDREAS S,JEAN H J.Multiple site-directed mutagenesis of more than 10 sites simultaneously and in a single round[J].Analy Biochem,2004,324:285-291.
  • 2LIU Xiang-mei,QU Yin-bo,FAN Yin,et al.Studies on the key amino acid residues responsible for the alkali-tolerance of the xylanase by site-directed or random mutagenesis[J].J Mol Catalysis B:Enzy,2002,18(4-6):307-313.
  • 3徐卉芳,张先恩,张治平,张用梅,A.E.G.CASS.大肠杆菌碱性磷酸酶的体外定向进化研究[J].生物化学与生物物理进展,2003,30(1):89-94. 被引量:13
  • 4VOIGT C A,KAUFFMAN S,WANG Zhen-gang.Rational evolutionary design:The theory of in vitro protein evolution[J].Adv Protein Chem,2001,55:79-160.
  • 5ROBERT J H,JORG B,MARIE L A,et al.Combining computational and experimental screening for rapid optimization of protein properties[J].Proc Natl Acad Sci USA,2002,99:15 926-15 931.
  • 6VOIGT C A,MAYO S L,ARNOLD F H,et al.Computational method to reduce the search space for directed protein evolution[J].Proc Natl Acad Sci USA,2001,98:3 778-3 783.
  • 7RICHARD F,AJOY R,SRIDHAR G,et al.Optimizing the search algorithm for protein engineering by directed evolution[J].Protein Eng,2003,16(8):589-597.
  • 8LIU Liang-wei,WANG Mei-li,SHAO Wei-lan,et al.A novel model to determine the dipeptides responsible for optimum temperature in F/10 xylanase[J].Process Biochem,2005,40(3):1 389-1 394.
  • 9LIU Liang-wei,ZHANG Jing,CHEN Bin,et al.Principle component analysis in F/10 and G/11 xylanase[J].Bioch Biophy Res Co,2004,322(1):277-280.

二级参考文献18

  • 1Arnold F H. Directed evolution: creating biocatalysts for the future. Chem Eng Sci, 1996, 51(23): 5091~5102
  • 2Stemmer W P C. Rapid evolution of a protein in vitro by DNA shuffling. Nature, 1994, 370(4): 389~391
  • 3Oue S, Okamoto A, Yano T, et al. Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J Biol Chem, 1999, 274(4): 2344~2349
  • 4Miyazaki K, Wintrode P L, Grayling R A, et al. Directed evolution study of temperature adaption in a psychrophilic enzyme. J Mol Biol, 2000, 297(4): 1015~1026
  • 5Kim E E, Wyckoff H W. Structure and function of alkaline phosphatases: structure of alkaline phosphatase. Clin Chim Acta, 1989, 186(1-2): 175~188
  • 6Holtz K M, Kantrowitz E R. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. FEBS Letters, 1999, 462(1): 7~11
  • 7Mandecki W, Shallcross M A, Sowadski J, et al. Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat. Protein Engig, 1991, 4(7): 801~804
  • 8Chen L, Neidhart D, Kohlbrenner W M, et al. 3-D structure of a mutant (Asp101→Ser) of E.coli alkaline phosphatase with higher catalytic activity. Protein Engig, 1992, 5(7): 605~610
  • 9Zhang X E, Zhou Y H, Zhang Z P, et al. Engineering E.coli alkaline phosphatase yields changes of catalytic activity, thermal stability and phosphate inhibition. Biocataly Biotransform, 2002, 20(6):381~389
  • 10Chaidaroglou A, Brezinski D J, Middleton S A, et al. Function of Arginine-166 in the active site of Escherichia coli alkaline phosphatase. Biochemistry, 1988, 27(22): 8338~8343

共引文献12

同被引文献12

  • 1URRY D W.Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers[J].Phys Chem (B),1997,101(51):11007-11028.
  • 2CHOW D,NUNALEE M L,CHILKOTI A,et al.Peptide-based biopolymers in biomedicine and biotechnology[J].Mater Sci Eng R Rep,2008,62(4):125-155.
  • 3URRY D W,LUAN C H,PARKER T M,et al.Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity[J].J Am Chem Soc,1991,113 (11):4346-4348.
  • 4MEYER D E,CHILKOTI A.Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides[J].Biomacromolecules,2004,5 (3):846-851.
  • 5OISON S D.Mathematical models for analysis of tissue regeneration in articular cartilage[D].North Carolina State:North Carolina State University,2009.
  • 6CHOU Kuo-chen.Prediction of protein cellular attributes using pseudo amino acid composition[J].Proteins:Structure,Function,and Bioinformatics,2001,43(3):246-255.
  • 7SHEN Hong-bin,CHOU Kuo-chen.PseAAC:A flexible web-server for generating various kinds of protein pseudo amino acid composition[J].Analytical Biochemistry,2008,373 (2):386-388.
  • 8VANPNIK V N.The nature of statistical learning theory[M].New York:Springer-Verlag,1995.
  • 9ROUSSEEUW P J.Least median of squares regression[J].Journal of the American Statistical Association,1984,79(388):871-880.
  • 10STEELE J M,STEIGER W L.Algorithms and complexity for least median of squares regression[J].Discrete Applied Mathematics,1986,14(1):93-100.

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