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Peptide Hydrophobicity/Hydrophilicity Analysis:

Sequence: (NH2-) 5-FAM 5-FAM-Ahx Acetylation Biotin Biotin-Ahx Br-Ac- CBZ Dansyl Dansyl-Ahx DTPA FITC FITC-Ahx Fmoc Formylation HYNIC MCA Myristoyl Palmitoyl PEN TMR (-COOH) AMC Amidation Bzl CMK Cysteamide Et FMK MAPS Asymmetric 4 branches MAPS Asymmetric 8 branches Me NHEt NHisopen NHMe OSU tBu Aldehyde Alcohol Ester (OMe) Ester (OEt) Other Modification: 1-Pyrenemethylamine HCLAbzAbz/DNPAbz/Tyr (3-NO2)Amide CyclicBOCDABCYLDABCYL/Glu(EDANS)-NH2Double Disulfide bridgeEDANS/DABCYLGlu(EDANS)-NH2MCA/DNPmini-PEG1mini-PEG2Mono Disulfide bridgeP-NitroanilideSuccinylationTriple Disulfide bridgeTyr (3-NO2)

Amino Acids Reference :
Amino Acids with Hydrophobic Side Chain - Aliphatic
Alanine, Ala, A	Isoleucine, Ile, I	Leucine, Leu, L
Valine, Val, V
Amino Acids with Hydrophobic Side Chain - Aromatic
Phenylalanine, Phe, F	Tryptophan, Trp, W	Tyrosine, Tyr, Y
Amino Acids with Polar Neutral Side Chains
Asparagine, Asn, N	Cysteine, Cys, C	Glutamine, Gln, Q
Methionine, Met, M	Serine, Ser, S	Threonine, Thr, T
Amino Acids with Electricaly Charged Side Chains - Acidic
Aspartic acid, Asp, D	Glutamic acid, Glu, E
Amino Acids with Electricaly Charged Side Chains - Basic
Arginine, Arg, R	Histidine, His, H	Lysine, Lys, K
Unique Amino Acids
Glycine, Gly, G	Proline, Pro, P
Properties of Common Amino Acids
Hydrophobicity Index for Common Amino Acids
The hydrophobicity index is a measure of the relative hydrophobicity, or how soluble an amino acid is in water. In a protein, hydrophobic amino acids are likely to be found in the interior, whereas hydrophilic amino acids are likely to be in contact with the aqueous environment. The values in the table below are normalized so that the most hydrophobic residue is given a value of 100 relative to glycine, which is considered neutral (0 value). The scales were extrapolated to residues which are more hydrophilic than glycine.