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Select Format of your Sequence Amino Acids only (single letter code) Standard Format (Readable by READSEQ)
Select Parameters (Maximum Four,Defauly % Exposed Residues):
Free energy of transfer to surface (Bull & Breese, Arch. Biophys. Biochem. 161, 665 (1974) ) Average accessibility surface area (Janin et al., J. Mol. Biol. 125, 357 (1978) ) Percentage of buried residues (Janin et al., J. Mol. Biol. 125, 357 (1978) ) Percentage of exposed residues (Janin et al., J. Mol. Biol. 125, 357 (1978) ) Hydrophobic index (Ponnuswamy et al., Biochim. Biophys. Acta 623, 301 (1980) ) Hydrophobicity in folded form (Ponnuswamy et al., BBA 623, 301 (1980) ) Hydrophobicity in unfolded form (Ponnuswamy et al., BBA 623, 301 (1980) ) Hydrophobicity gain (Ponnuswamy et al., BBA 623, 301 (1980) ) Polarity (Ponnuswamy et al., Biochim. Biophys. Acta 623, 301 (1980) ) Surrounding hydrophobicity in a-helix (Ponnuswamy et al., BBA 623, 301 (1980) ) Surrounding hydrophobicity in b-sheet (Ponnuswamy et al. BBA 623, 301 (1980) ) Surrounding hydrophobicity in b-turn (Ponnuswamy et al., BBA 623, 301 (1980) ) Accessibility reduction ratio (Ponnuswamy et al., BBA 623, 301 (1980) ) Average number of surrounding residues (Ponnuswamy BBA 623, 301 (1980) ) Volume (Chothia, Nature 254, 304 (1975) ) Local flexibility (Ragone et al. 1989) Flexibility (Bhaskaran and Ponnuswamy 1988) Flexibility for no rigid neighbours (Karplus & Schulz, Naturwiss. 72, 212 (1985) ) Flexibility for one rigid neighbour (Karplus & Schulz, Naturwiss. 72, 212 (1985) ) Flexibility for two rigid neighbours (Karplus & Schulz, Naturwiss. 72, 212 (1985) ) Hydrophobicity (Eisenberg, Ann. Rev. Biochem. 53, 595 (1984) ) Accessible surface area in the standard state (Rose et al., Sci. 229, 834 (1985) ) Average accessible surface area in folded proteins (Rose et al., Sci. 229, 834 (1985) ) Average surrounding hydrophobicity (Manavalan et al. Nature 275, 673 (1978) ) Hydrophilicity (Hopp and Woods, PNAS 78, 3824 (1981) ) Hydropathy (Kyte and Doolittle, J. Mol. Biol. 157, 105 (1982) ) Hydrophilicity from HPLC (Parker et al. Biochemistry 25, 5425 (1986) ) Hydrophobicity (Jones, J. Theor. Biol. 125, 357 (1975) ) Refractivity (Jones, J. Theor. Biol. 125, 357 (1975) ) Normalized frequency of a-helix with weights (Levitt, Biochem. 17, 4277 (1978) ) Normalized frequency of b-sheet with weights (Levitt, Biochem. 17, 4277 (1978) ) Normalized frequency for reverse turn with weights (Levitt, Biochem. 17, 4277 (1978) ) Barrell, Bankier and Drouin (1979) Signature for rapidly degraded proteins Charge of amino acids (example scale) Local concentration of aromatic amino acids
Moment Method: Direct/No Moment Unnormalized Moment Normalized Moment Smooth Moment Angle Moment Angle Face of Alpha Helix Face of beta-sheet Window Size (Default Size 7): 7 1 3 5 9 11 13 15 17 19 21 23 25
Averaging Method: Mean Over Window Hat Over Window Median Over Window Data Sieve Fourier Smoothing Window Size (Default Size 7): 7 1 3 5 9 11 13 15 17 19 21 23 25
Width of graph : Fixed Variable Presentation of Properties in Single Graph Multiple Graphs