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Cited by 283

The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.

ASAView: Database and tool for solvent accessibility representation in proteins

Open access
Ahmad, Shandar, Gromiha, Michael, Fawareh, Hamed, Sarai, Akinori·2004·BMC Bioinformatics

Abstract

BACKGROUND: Accessible surface area (ASA) or solvent accessibility of amino acids in a protein has important implications. Knowledge of surface residues helps in locating potential candidates of active sites. Therefore, a method to quickly see the surface residues in a two dimensional model would help to immediately understand the population of amino acid residues on the surface and in the inner core of the proteins. RESULTS: ASAView is an algorithm, an application and a database of schematic representations of solvent accessibility of amino acid residues within proteins. A characteristic two-dimensional spiral plot of solvent accessibility provides a convenient graphical view of residues in terms of their exposed surface areas. In addition, sequential plots in the form of bar charts are also provided. Online plots of the proteins included in the entire Protein Data Bank (PDB), are provided for the entire protein as well as their chains separately. CONCLUSIONS: These graphical plots of solvent accessibility are likely to provide a quick view of the overall topological distribution of residues in proteins. Chain-wise computation of solvent accessibility is also provided.

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Metadata

Authors
Ahmad, S., Gromiha, M., Fawareh, H., & Sarai, A.
Venue
BMC Bioinformatics
Published
2004-05-01
Volume
5
Issue
1
Pages
51-51
ISSN
1471-2105 (ISSN-L)
OpenAlex
W1747519124
Cited by
283
References
20
FWCI
1.20
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: ASAView: Database and tool for solvent accessibility representation in proteins. https://app.cochat.ai/papers/10.1186/1471-2105-5-51
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Ahmad, S., Gromiha, M., Fawareh, H., & Sarai, A. (2004). ASAView: Database and tool for solvent accessibility representation in proteins. BMC Bioinformatics. https://doi.org/10.1186/1471-2105-5-51

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