Analysis of a Protein Sequence (Result in Table Form)
PSAweb Server
Paste your protein sequence:
or Submit your sequence
Format of your Sequence
Amino acids only(single letter code)
Standard Format (Readable by READSEQ)
Select Parameters (Maximum Four parameters at a time)
:
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
Select Type of Presentation:
Graphical
Text
Select Property of Residues to be highlighted (Only for Text presentation)
Hydrophobic (A,C,F,G,H,I,K,L,M,T,V,W,Y)
Polar (C,D,E,H,K,N,Q,R,S,T,W,Y)
Small (A,C,D,G,N,P,S,T,V)
Proline (P)
Tiny (A,C,G,S)
Aliphatic (I,L,V)
Aromatic (F,H,Y,Y)
Positive (H,K,R)
Negative (D,E)
Charged (D,E,H,K,R)
Select Residues to be highlighted (Underline)
:
A
C
D
E
F
G
H
I
K
L
M
N
P
Q
R
S
T
V
W
Y