Literature DB >> 1404357

Predicting protein secondary structure with a nearest-neighbor algorithm.

S Salzberg1, S Cost.   

Abstract

We have developed a new method for protein secondary structure prediction that achieves accuracies as high as 71.0%, the highest value yet reported. The main component of our method is a nearest-neighbor algorithm that uses a more sophisticated treatment of the feature space than standard nearest-neighbor methods. It calculates distance tables that allow it to produce real-valued distances between amino acid residues, and attaches weights to the instances to further modify the the structure of feature space. The algorithm, which is closely related to the memory-based reasoning method of Zhang et al., is simple and easy to train, and has also been applied with excellent results to the problem of identifying DNA promoter sequences.

Mesh:

Year:  1992        PMID: 1404357     DOI: 10.1016/0022-2836(92)90892-n

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  14 in total

1.  Distinguishing between sequential and nonsequentially folded proteins: implications for folding and misfolding.

Authors:  C J Tsai; J V Maizel; R Nussinov
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

2.  Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements.

Authors:  Hamid R Eghbalnia; Liya Wang; Arash Bahrami; Amir Assadi; John L Markley
Journal:  J Biomol NMR       Date:  2005-05       Impact factor: 2.835

3.  Prediction of compounds' biological function (metabolic pathways) based on functional group composition.

Authors:  Yu-Dong Cai; Ziliang Qian; Lin Lu; Kai-Yan Feng; Xin Meng; Bing Niu; Guo-Dong Zhao; Wen-Cong Lu
Journal:  Mol Divers       Date:  2008-08-14       Impact factor: 2.943

4.  Improving protein secondary structure prediction with aligned homologous sequences.

Authors:  V Di Francesco; J Garnier; P J Munson
Journal:  Protein Sci       Date:  1996-01       Impact factor: 6.725

Review 5.  Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution.

Authors:  M H Saier
Journal:  Microbiol Rev       Date:  1994-03

6.  A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor design.

Authors:  A Wallqvist; R L Jernigan; D G Covell
Journal:  Protein Sci       Date:  1995-09       Impact factor: 6.725

7.  Improved prediction of protein secondary structure by use of sequence profiles and neural networks.

Authors:  B Rost; C Sander
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-15       Impact factor: 11.205

8.  Distributions of amino acids suggest that certain residue types more effectively determine protein secondary structure.

Authors:  S Saraswathi; J L Fernández-Martínez; A Koliński; R L Jernigan; A Kloczkowski
Journal:  J Mol Model       Date:  2013-08-02       Impact factor: 1.810

9.  The mannitol repressor (MtlR) of Escherichia coli.

Authors:  R M Figge; T M Ramseier; M H Saier
Journal:  J Bacteriol       Date:  1994-02       Impact factor: 3.490

10.  Fast learning optimized prediction methodology (FLOPRED) for protein secondary structure prediction.

Authors:  S Saraswathi; J L Fernández-Martínez; A Kolinski; R L Jernigan; A Kloczkowski
Journal:  J Mol Model       Date:  2012-05-08       Impact factor: 1.810

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