A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
- 11 April 1997
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 267 (4) , 1026-1038
- https://doi.org/10.1006/jmbi.1997.0924
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Protein fold recognition using sequence‐derived predictionsProtein Science, 1996
- Progress in fold recognitionProteins-Structure Function and Bioinformatics, 1995
- Comparison of conformational characteristics in structurally similar protein pairsProtein Science, 1993
- Three‐dimensional structural resemblance between the ribonuclease H and connection domains of HIV reverse transcriptase and the ATPase fold revealed using graph theoretical techniquesFEBS Letters, 1993
- An empirical energy function for threading protein sequence through the folding motifProteins-Structure Function and Bioinformatics, 1993
- Amino acid substitution matrices from protein blocks.Proceedings of the National Academy of Sciences, 1992
- Topology fingerprint approach to the inverse protein folding problemJournal of Molecular Biology, 1992
- Exhaustive Matching of the Entire Protein Sequence DatabaseScience, 1992
- A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional StructureScience, 1991
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977