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. 2000 May 18;249(1):53–65. doi: 10.1016/S0378-1119(00)00136-0

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Copyright © 2000 Elsevier Science B.V. All rights reserved.

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Fig. 1 — (A) Nucleotide and deduced amino acid sequence of GP73 (GenBank accession number AF236056). Two potential starting methionines are underlined. The presumptive transmembrane domain is underlined. Several O- or N-linked glycosylation consensus sites are marked by a caret (^). The stop codon is marked by asterisks. (B) Hydropathicity analysis of GP73. The hydropathicity analysis was carried out using the algorithm by Kyte and Doolittle. A hydrophobic stretch is present in the N-terminal portion of the protein, corresponding to a predicted membrane-spanning domain. The remainder of the protein is predicted to be hydrophilic. (C) Coiled coil analysis of GP73. The analysis was performed according to the algorithm by Lupas. The graph plots the likelihood for a given amino acid to be part of a coiled coil domain.

Fig. 1 — (A) Nucleotide and deduced amino acid sequence of GP73 (GenBank accession number AF236056). Two potential starting methionines are underlined. The presumptive transmembrane domain is underlined. Several O- or N-linked glycosylation consensus sites are marked by a caret (^). The stop codon is marked by asterisks. (B) Hydropathicity analysis of GP73. The hydropathicity analysis was carried out using the algorithm by Kyte and Doolittle. A hydrophobic stretch is present in the N-terminal portion of the protein, corresponding to a predicted membrane-spanning domain. The remainder of the protein is predicted to be hydrophilic. (C) Coiled coil analysis of GP73. The analysis was performed according to the algorithm by Lupas. The graph plots the likelihood for a given amino acid to be part of a coiled coil domain.