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Review
. 2008 Sep;148(1):6-24.
doi: 10.1104/pp.108.120725.

The enigmatic LEA proteins and other hydrophilins

Affiliations
Review

The enigmatic LEA proteins and other hydrophilins

Marina Battaglia et al. Plant Physiol. 2008 Sep.
No abstract available

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Figures

Figure 1.
Figure 1.
Graphic representation of LEA proteins according to the properties that define the hydrophilins. This analysis includes data for all LEA proteins considered in this work (378). All points on the top right quadrant correspond to proteins that can be considered as hydrophilins according to their definition (hydrophilicity index > 1, Gly > 6%). Also, 3,000 randomly chosen Arabidopsis proteins are shown as reference. To obtain the hydrophilicity index, the average hydrophobicity of all amino acids in the protein was multiplied by −1 (Kyte and Doolittle, 1982).
Figure 2.
Figure 2.
Protein size and fraction predicted as unstructured of LEA proteins belonging to different groups. Also, 3,000 randomly chosen Arabidopsis proteins are shown as reference. Many of them (1,350 of 3,000) cannot be seen because they overlap the x axis, as they were predicted to be 0% unstructured. The unstructured fraction was calculated according to Dosztányi et al. (2005), using a sliding window of 21 amino acids.
Figure 3.
Figure 3.
Array of the distinctive motifs in the LEA protein groups. Each block contains a schematic representation of the arrangement of the motifs that distinguish each group of LEA proteins and their corresponding subgroups. Although similar colors and numbers indicate the different motifs for each group, they do not imply any sequence relation among the motifs in the different blocks. The amino acid sequence corresponding to each motif represented here is shown in Table II. The range of protein sizes in each group is indicated at the top of each block, in number of amino acid (aa) residues.

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