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Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
Open accessAbstract
The present paper describes the SSM algorithm of protein structure comparison in three dimensions, which includes an original procedure of matching graphs built on the protein's secondary-structure elements, followed by an iterative three-dimensional alignment of protein backbone Calpha atoms. The SSM results are compared with those obtained from other protein comparison servers, and the advantages and disadvantages of different scores that are used for structure recognition are discussed. A new score, balancing the r.m.s.d. and alignment length Nalign, is proposed. It is found that different servers agree reasonably well on the new score, while showing considerable differences in r.m.s.d. and Nalign.
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Cites
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
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US-align: universal structure alignments of proteins, nucleic acids, and macromolecular complexes
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Metadata
- Authors
- Krissinel, E., & Henrick, K.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 2004-11-26
- Volume
- 60
- Issue
- 12
- Pages
- 2256-2268
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2144998676
- Cited by
- 3,760
- References
- 1
- FWCI
- 32.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Krissinel, E., & Henrick, K. (2004). Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallographica Section D Biological Crystallography. https://doi.org/10.1107/s0907444904026460
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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