Literature DB >> 26396655

Statistical approach for lysosomal membrane proteins (LMPs) identification.

Vijay Tripathi1, Pooja Tripathi2, Dwijendra Gupta3.   

Abstract

Discrimination of Lysosomal membrane proteins (LMP's) from folding types of globular (GPs) and other membrane proteins (OtMPs) is an important task both for identifying LMPs from genomic sequences and for the successful prediction of their secondary and tertiary structures. We have systematically analyzed the amino acid frequencies as well as dipeptide count of GPs, LMPs and OtMPs. Based on the above calculated single amino acid frequency combined with dipeptide count information, we statistically discriminated LMPs from GPs and OtMPs. This approach correctly classified the LMPs with an accuracy of 95 %. On the other hand, the amino acid frequency alone can discriminate LMPs with an accuracy of only 79 %. Similarly dipeptide count alone has an accuracy of 87 % for the discrimination of LMPs. Thus the combined information of both amino acid frequencies and dipeptide composition gives us significant high accurate results.

Entities:  

Keywords:  Amino acid frequency; Dipeptide composition; Globular proteins; Lysosomal membrane proteins; Other membrane proteins

Year:  2014        PMID: 26396655      PMCID: PMC4571724          DOI: 10.1007/s11693-014-9153-7

Source DB:  PubMed          Journal:  Syst Synth Biol        ISSN: 1872-5325


  16 in total

1.  The Protein Data Bank.

Authors:  H M Berman; J Westbrook; Z Feng; G Gilliland; T N Bhat; H Weissig; I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

2.  High-resolution structure of the OmpA membrane domain.

Authors:  A Pautsch; G E Schulz
Journal:  J Mol Biol       Date:  2000-04-28       Impact factor: 5.469

3.  Evaluation and improvement of multiple sequence methods for protein secondary structure prediction.

Authors:  J A Cuff; G J Barton
Journal:  Proteins       Date:  1999-03-01

4.  Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.

Authors:  L Vandeputte-Rutten; R A Kramer; J Kroon; N Dekker; M R Egmond; P Gros
Journal:  EMBO J       Date:  2001-09-17       Impact factor: 11.598

5.  Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution.

Authors:  K Zeth; K Diederichs; W Welte; H Engelhardt
Journal:  Structure       Date:  2000-09-15       Impact factor: 5.006

6.  Application of SVM to predict membrane protein types.

Authors:  Yu-Dong Cai; Pong-Wong Ricardo; Chih-Hung Jen; Kuo-Chen Chou
Journal:  J Theor Biol       Date:  2004-02-21       Impact factor: 2.691

7.  A simple statistical method for discriminating outer membrane proteins with better accuracy.

Authors:  M Michael Gromiha; Makiko Suwa
Journal:  Bioinformatics       Date:  2004-11-05       Impact factor: 6.937

8.  Application of residue distribution along the sequence for discriminating outer membrane proteins.

Authors:  M Michael Gromiha; Shandar Ahmad; Makiko Suwa
Journal:  Comput Biol Chem       Date:  2005-04       Impact factor: 2.877

9.  Using stacked generalization to predict membrane protein types based on pseudo-amino acid composition.

Authors:  Shuang-Quan Wang; Jie Yang; Kuo-Chen Chou
Journal:  J Theor Biol       Date:  2006-05-16       Impact factor: 2.691

10.  Discriminating lysosomal membrane protein types using dynamic neural network.

Authors:  Vijay Tripathi; Dwijendra Kumar Gupta
Journal:  J Biomol Struct Dyn       Date:  2013-08-22
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