Additional file 8: Figure S3. Correlation of amino acid hydrophobicity distance to evolution scale and separation capacity score of real hydrophobicity scale. Shown is the correlation via linear fit between the separation capacity for the 98 real hydrophobicity scales and the distance of hydrophobicity value of a single amino acid to the in silico evolved scale. The single amino acids are distributed to four graphs (AâD) concerning their slope of the individual linear fit. (A) Raising slope red; (B) slightly raising slope blue; (C) no raising slope black; (D) falling slope green
<p>Evolution of the ratio between the atomic hydrophobicity and the total molecular surface area (hy...
Hydrophobicity is one of the main attributes of amino acid side-chains. Hundreds of different hydrop...
Figure S3. Lengths and hydrophobicities of sequences that were not predicted. Upper: Sequence length...
Additional file 7: Figure S2. Normalized amino acid hydrophobicity values of evolved scale. Shown is...
Background: Physicochemical properties are frequently analyzed to characterize protein-sequences of ...
Additional file 11: Table S7. Influence of convex envelope on volume and number of peptides. Represe...
BACKGROUND: Physicochemical properties are frequently analyzed to characterize protein-sequences of ...
Additional file 4: Table S3. Amino acid composition in sequence pools. Given are the sequence pool (...
Partition coefficients, expressed as logP, were calculated using Advanced Chemistry Development soft...
a<p>Mw: molecular weight in Daltons.</p>b<p>H: the hydrophobicity per residue of peptides calculated...
In spite of its relevant biological role, no general consensus exists on the quantitative characteri...
<p><b>Notes:</b></p><p>1. Overall hydrophobicity is the algebraic sum of hydrophilicity (positive si...
Hydrophobic/hydrophilic character of an amino acid, an important property in protein structure and p...
Hydrophobicity is one of the most important physicochemical properties of proteins. Moreover, it pla...
(A) A model peptide with an arginine at the central position (green) is shown spanning a low-dielect...
<p>Evolution of the ratio between the atomic hydrophobicity and the total molecular surface area (hy...
Hydrophobicity is one of the main attributes of amino acid side-chains. Hundreds of different hydrop...
Figure S3. Lengths and hydrophobicities of sequences that were not predicted. Upper: Sequence length...
Additional file 7: Figure S2. Normalized amino acid hydrophobicity values of evolved scale. Shown is...
Background: Physicochemical properties are frequently analyzed to characterize protein-sequences of ...
Additional file 11: Table S7. Influence of convex envelope on volume and number of peptides. Represe...
BACKGROUND: Physicochemical properties are frequently analyzed to characterize protein-sequences of ...
Additional file 4: Table S3. Amino acid composition in sequence pools. Given are the sequence pool (...
Partition coefficients, expressed as logP, were calculated using Advanced Chemistry Development soft...
a<p>Mw: molecular weight in Daltons.</p>b<p>H: the hydrophobicity per residue of peptides calculated...
In spite of its relevant biological role, no general consensus exists on the quantitative characteri...
<p><b>Notes:</b></p><p>1. Overall hydrophobicity is the algebraic sum of hydrophilicity (positive si...
Hydrophobic/hydrophilic character of an amino acid, an important property in protein structure and p...
Hydrophobicity is one of the most important physicochemical properties of proteins. Moreover, it pla...
(A) A model peptide with an arginine at the central position (green) is shown spanning a low-dielect...
<p>Evolution of the ratio between the atomic hydrophobicity and the total molecular surface area (hy...
Hydrophobicity is one of the main attributes of amino acid side-chains. Hundreds of different hydrop...
Figure S3. Lengths and hydrophobicities of sequences that were not predicted. Upper: Sequence length...