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Cited by 618

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences

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Gaboriaud, C., Bissery, V., Benchetrit, T., Mornon, J.P.·1987·FEBS Letters

Abstract

A new method for comparing and aligning protein sequences is described. This method, hydrophobic cluster analysis (HCA), relies upon a two‐dimensional (2D) representation of the sequences. Hydrophobic clusters are determined in this 2D pattern and then used for the sequence comparisons. The method does not require powerful computer resources and can deal with distantly related proteins, even if no 3D data are available. This is illustrated in the present report by a comparison of human haemoglobin with leghaemoglobin, a comparison of the two domains of liver rhodanese (thiosulphate sulphurtransferase) and a comparison of plastocyanin and azurin.

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Metadata

Authors
Gaboriaud, C., Bissery, V., Benchetrit, T., & Mornon, J. P.
Venue
FEBS Letters
Publisher
Wiley
Published
1987-11-16
Volume
224
Issue
1
Pages
149-155
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1972961211
Cited by
618
References
1
FWCI
4.62
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences. https://app.cochat.ai/papers/10.1016/0014-5793(87)80439-8
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Gaboriaud, C., Bissery, V., Benchetrit, T., & Mornon, J. P. (1987). Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences. FEBS Letters. https://doi.org/10.1016/0014-5793(87)80439-8

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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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