STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins
Open accessAbstract
STRIDE is a software tool for secondary structure assignment from atomic resolution protein structures. It implements a knowledge-based algorithm that makes combined use of hydrogen bond energy and statistically derived backbone torsional angle information and is optimized to return resulting assignments in maximal agreement with crystallographers' designations. The STRIDE web server provides access to this tool and allows visualization of the secondary structure, as well as contact and Ramachandran maps for any file uploaded by the user with atomic coordinates in the Protein Data Bank (PDB) format. A searchable database of STRIDE assignments for the latest PDB release is also provided. The STRIDE server is accessible from http://webclu.bio.wzw.tum.de/stride/.
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STRIDE identifies α-helix for residues 261-268 and 3-10 helix for residues 277-280 in the lowest energy conformation of Tau(254-290).
“Analysis of secondary structure in the lowest energy conformation using STRIDE47, identifies α-helix for residues 261–268 and 3–10 helix for residues 277–280.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [47]
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- Authors
- Heinig, M., & Frishman, D.
- Affiliations
- Technical University of Munich (DE)
- Corresponding author
- Heinig, M.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-07-01
- Volume
- 32
- Issue
- Web Server
- Pages
- W500-W502
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC441567
- OpenAlex
- W2133179696
- Cited by
- 1,003
- References
- 0
- Citations by year
- 2026: 52 · 2025: 63 · 2024: 65 · 2023: 70 · 2022: 72 · 2021: 73 · 2020: 76 · 2019: 55 · 2018: 48 · 2017: 43 · 2016: 54 · 2015: 54 · 2014: 50 · 2013: 52 · 2012: 47
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- other-oa
- Locations
- Nucleic Acids Research (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- secondary structure assignment, protein structure, hydrogen bond strength, Ramachandran map, contact maps, Protein Data Bank, web server
- MeSH terms
- Hydrogen Bonding, Proteins, Software, Molecular Structure, Protein Structure, Secondary, Internet, Databases, Protein
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