1984
DOI: 10.1016/0022-2836(84)90309-7
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Analysis of membrane and surface protein sequences with the hydrophobic moment plot

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Cited by 2,171 publications
(1,388 citation statements)
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References 52 publications
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“…IB). 0.57 and 0.52, well above the threshold value of 0.42 used by Eisenberg et al (1984) to identify potential transmembrane segments. Thus, combining information from sequence analysis and the crystal structure, we infer that the T domain has 4 potential transmembrane helices (residues 269-289, 301-321, 328-348, and 351-371).…”
Section: Transmembrane Domainmentioning
confidence: 88%
“…IB). 0.57 and 0.52, well above the threshold value of 0.42 used by Eisenberg et al (1984) to identify potential transmembrane segments. Thus, combining information from sequence analysis and the crystal structure, we infer that the T domain has 4 potential transmembrane helices (residues 269-289, 301-321, 328-348, and 351-371).…”
Section: Transmembrane Domainmentioning
confidence: 88%
“…The mathematical tools used for this purpose are analogous to those originally developed for protein a-helices, such as the helical wheel diagrams of Schiffer and Edmundson [33] and the hydrophobic moment of Eisenberg and co-workers [34,35]. Applying this formalism to the bendability distribution in DNA we found that intrinsically curved sites seem to have an asymmetric, helically phased bendability pattern.…”
Section: Patterns Of Bendability In Dna Sequencesmentioning
confidence: 95%
“…Using the normalised consensus hydrophobicity scale of Eisenberg et al, 52 and a moving window of 11 residues, the window in the sequence of MH5 with the highest value of < µH > was computed along with its mean hydrophobicity, < H >. Using these values of < µH > and < H > as coordinates, a data point representing MH5 was plotted on the hydrophobic moment plot diagram of Eisenberg et al 50 , as modified by Harris et al 53 , to identify candidate tilted α-helix forming segments. Graphical representation of MH5 as a two-dimensional axial projection 8 taken perpendicular to the helical long axis and assuming an amino acid periodicity of 100° was undertaken according to the methodology of Schiffer and Edmundson 54 .…”
Section: Theoretical Analyses Of Mh5 -mentioning
confidence: 99%