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Graphical Representation of Peptide Physiochemical Properties



Peptide Sequence:SASAFFGMSRIGMEV

Charge
SASAFFGMSRIGMEV
P+veN-veNOC No charge
Polarity
SASAFFGMSRIGMEV
PHydrophobicNhydrophilic

Amino Acid Composition1400714140700140007210700Amino AcidACDEFGHIKLMNPQRSTVWY0510152025Amino Acid % Composition of Peptide Export to raster or vector imagePrint the chart
Hydrophobicity("JURD980101")HydrophobicitySASAFFGMSRIGMEV0-7.5-5-2.52.55Hydrophobicity Export to raster or vector imagePrint the chart
Preference for beta-strandsPreference for beta-strandsSASAFFGMSRIGMEV00.250.50.7511.251.51.75Preference for beta-strands Export to raster or vector imagePrint the chart
Frequency of alpha-helix in alpha/beta classFrequency of alpha-helix in alpha/beta classSASAFFGMSRIGMEV00.250.50.7511.251.51.75Frequency of alpha-helix in alpha/beta class Export to raster or vector imagePrint the chart
Physicochemical Properties of peptideHydrophobicity("JURD980101")Preference for beta-strandsfrequency of alpha-helix in alpha/beta classSASAFFGMSRIGMEV0.40.60.811.21.41.6Frequency of alpha-helix0-7.5-5-2.52.557.5Preference for beta-strands10.50.751.251.51.752Hydrophobicity Export to raster or vector imagePrint the chart


Amino Acid PolarityHydrophobicHydrophilic
8(53 %)7 (47 %)

Amino Acid Charge+vely charged-vely chargedNeutral Amino acid
1(6 %)1(6 %)13 (88 %)

Amino Acid Surface exposureSurface exposedBurried
5(33 %)10 (67 %)

DisorderDisorder-promotingOrder-promotingDisorder-order neutral
9(69 %)4(26 %)2 (5 %)

FlexibilityHighly flexibilityLow flexibility
5(33 %)10 (67 %)