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Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method

Cserzo, M., Wallin, E., Simon, I., von Heijne, G., Elofsson, A.·1997·Protein Engineering Design and Selection

Abstract

A new, simple method for predicting transmembrane segments in integral membrane proteins has been developed. It is based on low-stringency dot-plots of the query sequence against a collection of non-homologous membrane proteins using a previously derived scoring matrix [Cserzö et al., 1994, J. Mol. Biol., 243, 388-396]. This so-called dense alignment surface (DAS) method is shown to perform on par with earlier methods that require extra information in the form of multiple sequence alignments or the distribution of positively charged residues outside the transmembrane segments, and thus improves prediction abilities when only single-sequence information is available or for classes of membrane proteins that do not follow the 'positive inside' rule.

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Metadata

Authors
Cserzo, M., Wallin, E., Simon, I., von Heijne, G., & Elofsson, A.
Venue
Protein Engineering Design and Selection
Published
1997-06-01
Volume
10
Issue
6
Pages
673-676
ISSN
  • 0269-2139 (ISSN-L)
  • 1741-0126
  • 1741-0134
OpenAlex
W2115840790
Cited by
1,034
References
0
FWCI
8.32
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. https://app.cochat.ai/papers/10.1093/protein/10.6.673
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Cserzo, M., Wallin, E., Simon, I., von Heijne, G., & Elofsson, A. (1997). Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Engineering Design and Selection. https://doi.org/10.1093/protein/10.6.673

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.