<p>The profile for the Wimley-White scale was plotted using Mpex v. 3.2.6. The profile for the Eisenberg scale was plotted using ProtScale. Green areas correspond to identified cholesterol-binding motifs. Dark squares represent residues involved in the formation of salt-bridges. The light-blue graph corresponds to hydrophobic moment. Orange dots represent all of the histidine residues in the MPP1 sequence, which were assumed as uncharged. According to the Wimley-White scale, sequence fragment LPALQMFMR (156–164), apart from its last two residues, is located in a possible membrane-penetration region (indicated by the red line).</p
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
<p>The mean net charge (R) is plotted against the mean hydrophobicity (H). The boundary line is desc...
<p>All molecules are shown at their optimal position in the IMPALA slab after they were systematical...
<p>Almost all fragments (except one, residues 423–434) contain more than one possible cholesterol-bi...
Kyte and Doolittle Hydrophobicity plot derived from the MAP2191 (A) and FAP-P (B) conserved amino ac...
Hydrophobicity – fear of water – drives the folding of soluble proteins into their final folded stat...
Hydrophobicity – fear of water – drives the folding of soluble proteins into their final folded stat...
Integral membrane proteins often possess lipophilic a-helical regions of approximately 21 amino acid...
<p>(A) Amino-acid sequence of the ALPS motif of Nup133. The strongest hydrophobic region is highligh...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
<p>Color indicates the protein family (black: PfEMP1, gray: RIFIN, light gray: STEVOR). Error bars g...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
New membrane-preference scales are introduced for categories of membrane proteins with different fun...
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
<p>The mean net charge (R) is plotted against the mean hydrophobicity (H). The boundary line is desc...
<p>All molecules are shown at their optimal position in the IMPALA slab after they were systematical...
<p>Almost all fragments (except one, residues 423–434) contain more than one possible cholesterol-bi...
Kyte and Doolittle Hydrophobicity plot derived from the MAP2191 (A) and FAP-P (B) conserved amino ac...
Hydrophobicity – fear of water – drives the folding of soluble proteins into their final folded stat...
Hydrophobicity – fear of water – drives the folding of soluble proteins into their final folded stat...
Integral membrane proteins often possess lipophilic a-helical regions of approximately 21 amino acid...
<p>(A) Amino-acid sequence of the ALPS motif of Nup133. The strongest hydrophobic region is highligh...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
<p>Color indicates the protein family (black: PfEMP1, gray: RIFIN, light gray: STEVOR). Error bars g...
Hydropathy plots of amino acid sequences reveal the approximate locations of the transbilayer helice...
New membrane-preference scales are introduced for categories of membrane proteins with different fun...
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
The Eisenberg plot or hydrophobic moment plot methodology is one of the most frequently used methods...
<p>The mean net charge (R) is plotted against the mean hydrophobicity (H). The boundary line is desc...