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Protein fold recognition

T. Huber and A.E. Torda, Protein fold recognition without Boltzmann statistics or explicit physical basis, submitted to Protein Sci. (1997). [Pg.223]

Jones D T, W R Taylor and J M Thornton 1992. A New Approach to Protein Fold Recognition. Nature 358 86-89. [Pg.576]

DT Jones. Genthreader An efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol 287 797-815, 1999. [Pg.302]

DT Jones, WR Taylor, JM Thornton. A new approach to protein fold recognition. Nature 358 86-89, 1992. [Pg.303]

AE Torda. Perspectives in protein-fold recognition. Curr Opm Struct Biol 7 200-205, 1997. [Pg.303]

M Levitt. Competitive assessment of protein fold recognition and alignment accuracy. Proteins Suppl 1 92-104, 1997. [Pg.303]

D Eischer, D Eisenberg. Protein fold recognition using sequence-derived predictions. Protein Sci 5 947-955, 1996. [Pg.347]

B Rost, R Schneider, C Sander. Protein fold recognition by prediction-based threading. J Mol Biol 270 471-480, 1997. [Pg.347]

Rice, D.W., et al. A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. /. Mol. Biol. 267 1026-1038, 1997. [Pg.372]

PROTEIN FOLD RECOGNITION USING SEQUENCE PROFILES AND ITS APPLICATION IN STRUCTURAL GENOMICS... [Pg.245]

PROTEIN FOLD RECOGNITION USING SEQUENCE PROFILES... [Pg.247]

Fig. 3. The protein fold recognition protocol and fold prediction for complete genomes, (a) Construction of the FID library (b) fold prediction for proteins encoded in complete genomes. [Pg.259]

The 3D-PSSM (Kelley et ah, 2000) server at http //www.bmm.icnet.uk/ 3dpssm/ offers online protein fold recognition. On the submission form, enter your e-mail address and a one-line description of the query protein, then paste the query sequence into the sequence box and click the Submit button. The query sequence is used to search the Fold library for homologues. You will be informed of the URL where the result is located for 4 days. The output includes a summary table (hits with statistics models that can be viewed with RasMol classifications and links) and fold recognition by 3D-PSSM with a printout as exemplified in Figure 12.13. The alignment displays consensus sequence, secondary structures (C for coil, E for extended, and H for helix), and core score (0 for exterior to 9 for interior core). [Pg.254]

Figure 12.13. Protein fold recognition by 3D PSSB. The summary fold recognition results of cod alcohol dehydrogenase analyzed by 3D PSSB (secondary structure predic-... Figure 12.13. Protein fold recognition by 3D PSSB. The summary fold recognition results of cod alcohol dehydrogenase analyzed by 3D PSSB (secondary structure predic-...
PSIPRED Automatic sequence alignment, protein fold recognition, and secondary structure prediction web server 173 bioinf.cs.ucl.ac.uk/psipred/... [Pg.444]

The correctness of hits corresponding to families with known structural information is further verified by employing the protein fold recognition method PHYRE (Protein Homology/analogY Recognition Engine) version 0.2, which assesses the compatibility of a sequence to a three-dimensional structure (29). [Pg.158]

The commonly used benchmark for protein fold recognition is the test set suggested by Fischer et al. (1996), which comprises a set of 68 pairs of proteins with very low sequence similarity, but very highly similar folds. [Pg.97]


See other pages where Protein fold recognition is mentioned: [Pg.576]    [Pg.372]    [Pg.201]    [Pg.245]    [Pg.21]    [Pg.237]    [Pg.242]    [Pg.254]    [Pg.257]    [Pg.101]    [Pg.57]    [Pg.154]    [Pg.652]   


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