Neural network based prediction of protein structure and Function: Comparison with other machine learning methods

We have utilized neural networks in different applications of bioinformatics such as discrimination of beta-barrel membrane proteins, mesophilic and thermophilic proteins, different folding types of globular proteins, different classes of transporter proteins and predicting the secondary structures of beta-barrel membrane proteins. In these methods, we have used the information about amino acid composition, neighboring residue information, inter-residue contacts and amino acid properties as features. We observed that the performance with neural networks is comparable to or better than other widely used machine learning techniques.

[1]  J. Gibrat,et al.  Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs. , 1987, Journal of molecular biology.

[2]  M. Gromiha,et al.  Real value prediction of solvent accessibility from amino acid sequence , 2003, Proteins.

[3]  T. Sejnowski,et al.  Predicting the secondary structure of globular proteins using neural network models. , 1988, Journal of molecular biology.

[4]  Kuang Lin,et al.  A simple and fast secondary structure prediction method using hidden neural networks , 2005, Bioinform..

[5]  M. Gromiha,et al.  Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction. , 2001, Journal of molecular biology.

[6]  K. Burrage,et al.  Protein contact prediction using patterns of correlation , 2004, Proteins.

[7]  Robert M. MacCallum,et al.  Striped sheets and protein contact prediction , 2004, ISMB/ECCB.

[8]  C Sander,et al.  Third generation prediction of secondary structures. , 2000, Methods in molecular biology.

[9]  Shandar Ahmad,et al.  Application of residue distribution along the sequence for discriminating outer membrane proteins , 2005, Comput. Biol. Chem..

[10]  J Skolnick,et al.  Defrosting the frozen approximation: PROSPECTOR— A new approach to threading , 2001, Proteins.

[11]  Jagath C Rajapakse,et al.  Two‐stage support vector regression approach for predicting accessible surface areas of amino acids , 2006, Proteins.

[12]  H Naderi-Manesh,et al.  Prediction of protein surface accessibility with information theory. , 2000, Proteins.

[13]  P Fariselli,et al.  Prediction of contact maps with neural networks and correlated mutations. , 2001, Protein engineering.

[14]  C. Anfinsen Principles that govern the folding of protein chains. , 1973, Science.

[15]  Shandar Ahmad,et al.  Neural network‐based prediction of transmembrane β‐strand segments in outer membrane proteins , 2004, J. Comput. Chem..

[16]  Bin-Guang Ma,et al.  Direct correlation between proteins' folding rates and their amino acid compositions: An ab initio folding rate prediction , 2006, Proteins.

[17]  Chartchalerm Isarankura-Na-Ayudhya,et al.  Prediction of GFP spectral properties using artificial neural network , 2007, J. Comput. Chem..

[18]  David C. Jones,et al.  GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. , 1999, Journal of molecular biology.

[19]  M. Michael Gromiha,et al.  FOLD-RATE: prediction of protein folding rates from amino acid sequence , 2006, Nucleic Acids Res..

[20]  P K Ponnuswamy,et al.  A study of the preferred environment of amino acid residues in globular proteins. , 1977, Archives of biochemistry and biophysics.

[21]  M Michael Gromiha,et al.  Motifs in outer membrane protein sequences: applications for discrimination. , 2005, Biophysical chemistry.

[22]  M. Gromiha,et al.  Important inter-residue contacts for enhancing the thermal stability of thermophilic proteins. , 2001, Biophysical chemistry.

[23]  B. Rost,et al.  Conservation and prediction of solvent accessibility in protein families , 1994, Proteins.

[24]  M. Michael Gromiha,et al.  A Statistical Model for Predicting Protein Folding Rates from Amino Acid Sequence with Structural Class Information , 2005, J. Chem. Inf. Model..

[25]  Makiko Suwa,et al.  Neural network-based prediction of transmembrane beta-strand segments in outer membrane proteins. , 2004, Journal of computational chemistry.

[26]  Shandar Ahmad,et al.  Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information , 2004, Bioinform..

[27]  Shandar Ahmad,et al.  TMBETA-NET: discrimination and prediction of membrane spanning β-strands in outer membrane proteins , 2005, Nucleic Acids Res..

[28]  W. Goddard,et al.  First principles prediction of protein folding rates. , 1999, Journal of molecular biology.

[29]  M. Michael Gromiha,et al.  A Statistical Method for Predicting Protein Unfolding Rates from Amino Acid Sequence. , 2006 .

[30]  M Michael Gromiha,et al.  Important amino acid properties for determining the transition state structures of two‐state protein mutants , 2002, FEBS letters.

[31]  Lars Malmström,et al.  Automated prediction of CASP‐5 structures using the Robetta server , 2003, Proteins.

[32]  David R. Westhead,et al.  TMB-Hunt: a web server to screen sequence sets for transmembrane β-barrel proteins , 2005, Nucleic Acids Res..

[33]  T. Blundell,et al.  Comparative protein modelling by satisfaction of spatial restraints. , 1993, Journal of molecular biology.

[34]  Stavros J. Hamodrakas,et al.  Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method , 2005, BMC Bioinformatics.

[35]  M Michael Gromiha,et al.  Inter-residue interactions in protein folding and stability. , 2004, Progress in biophysics and molecular biology.

[36]  Piero Fariselli,et al.  A sequence-profile-based HMM for predicting and discriminating beta barrel membrane proteins , 2002, ISMB.

[37]  P. Y. Chou,et al.  Prediction of protein conformation. , 1974, Biochemistry.

[38]  M Michael Gromiha,et al.  Discrimination of mesophilic and thermophilic proteins using machine learning algorithms , 2007, Proteins.

[39]  M. Gromiha,et al.  Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. , 1999, Biophysical chemistry.

[40]  Makiko Suwa,et al.  Current developments on beta-barrel membrane proteins: sequence and structure analysis, discrimination and prediction. , 2007, Current protein & peptide science.

[41]  Makiko Suwa,et al.  Influence of amino acid properties for discriminating outer membrane proteins at better accuracy. , 2006, Biochimica et biophysica acta.

[42]  George D. Rose,et al.  Prediction of chain turns in globular proteins on a hydrophobic basis , 1978, Nature.

[43]  M. Kanehisa,et al.  Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins. , 1996, Protein engineering.

[44]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[45]  Harpreet Kaur,et al.  Prediction of transmembrane regions of beta-barrel proteins using ANN- and SVM-based methods. , 2004, Proteins.

[46]  Liang-Tsung Huang,et al.  iPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations , 2007, Bioinform..

[47]  P. Ponnuswamy,et al.  Hydrophobic character of amino acid residues in globular proteins , 1978, Nature.

[48]  Alan F. Murray,et al.  International Joint Conference on Neural Networks , 1993 .

[49]  Paul Horton,et al.  Discrimination of outer membrane proteins using support vector machines , 2005, Bioinform..

[50]  M. Gromiha,et al.  Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations. , 1999, Protein engineering.

[51]  Milton H. Saier,et al.  TCDB: the Transporter Classification Database for membrane transport protein analyses and information , 2005, Nucleic Acids Res..

[52]  Piero Fariselli,et al.  Predicting protein stability changes from sequences using support vector machines , 2005, ECCB/JBI.

[53]  B. Rost,et al.  Prediction of protein secondary structure at better than 70% accuracy. , 1993, Journal of molecular biology.

[54]  Y-h. Taguchi,et al.  Application of amino acid occurrence for discriminating different folding types of globular proteins , 2007, BMC Bioinformatics.

[55]  M. Michael Gromiha,et al.  A simple statistical method for discriminating outer membrane proteins with better accuracy , 2005, Bioinform..

[56]  Makiko Suwa,et al.  Discrimination of outer membrane proteins using machine learning algorithms , 2006, Proteins.

[57]  John Hallam,et al.  IEEE International Joint Conference on Neural Networks , 2005 .