*** mRMR features ***
Score Position Name
0.319 9 Hydropathy scale based on self-information values in the two-state model
0.033 7 Normalized frequency of beta-turn (Chou-Fasman 1978b)
0.024 7 alpha-CH chemical shifts (Andersen et al. 1992)
0.009 7 Hydrophobicity factor (Goldsack-Chalifoux 1973)
0.029 9 Negative charge (Fauchere et al. 1988)
-0.010 7 Relative preference value at N' (Richardson-Richardson 1988)
0.002 9 Loss of Side chain hydropathy by helix formation (Roseman 1988)
-0.008 7 Normalized frequency of beta-sheet unweighted (Levitt 1978)
-0.009 9 Helix termination parameter at posision j+1 (Finkelstein et al. 1991)
-0.013 7 Normalized frequency of N-terminal non beta region (Chou-Fasman 1978b)
-0.014 9 A parameter of charge transfer capability (Charton-Charton 1983)
-0.019 9 Linker propensity from long dataset (linker length is greater than 14
-0.017 7 The Chou-Fasman parameter of the coil conformation (Charton-Charton 1983)
-0.014 7 Propensity of amino acids within pi-helices (Fodje-Al-Karadaghi 2002)
0.002 9 Normalized composition from fungi and plant (Nakashima et al. 1990)
-0.019 9 Helix termination parameter at posision j-2j-1j (Finkelstein et al. 1991)
-0.016 9 Relative preference value at Mid (Richardson-Richardson 1988)
-0.017 7 Normalized frequency of chain reversal D (Tanaka-Scheraga 1977)
-0.012 9 Normalized relative frequency of double bend (Isogai et al. 1980)
-0.015 7 Turn propensity scale for transmembrane helices (Monne et al. 1999)
-0.009 9 Relative preference value at N1 (Richardson-Richardson 1988)
-0.020 9 Linker propensity from small dataset (linker length is less than six
-0.021 7 Normalized frequency of beta-sheet (Crawford et al. 1973)
-0.017 9 Normalized positional residue frequency at helix termini N2 (Aurora-Rose
-0.022 7 Normalized frequency of beta-sheet in alpha/beta class (Palau et al. 1981)
-0.019 9 Linker propensity from 3-linker dataset (George-Heringa 2003)
-0.015 9 Linker propensity from 1-linker dataset (George-Heringa 2003)
-0.015 9 Average relative fractional occurrence in E0(i-1) (Rackovsky-Scheraga 1982)
-0.016 7 Hydrophilicity scale (Kuhn et al. 1995)
-0.011 9 Normalized positional residue frequency at helix termini N" (Aurora-Rose
-0.012 9 Normalized positional residue frequency at helix termini N1 (Aurora-Rose
-0.014 7 Normalized positional residue frequency at helix termini N"' (Aurora-Rose
-0.017 9 Average relative fractional occurrence in EL(i) (Rackovsky-Scheraga 1982)
-0.017 9 Normalized frequency of N-terminal non helical region (Chou-Fasman 1978b)
-0.015 7 Average gain ratio in surrounding hydrophobicity (Ponnuswamy et al. 1980)
-0.013 9 The number of atoms in the side chain labelled 3+1 (Charton-Charton 1983)
-0.014 9 Relative preference value at N5 (Richardson-Richardson 1988)
-0.014 7 Normalized frequency of chain reversal (Tanaka-Scheraga 1977)
-0.011 9 Normalized frequency of reverse turn unweighted (Levitt 1978)
-0.013 9 Linker propensity from 2-linker dataset (George-Heringa 2003)
-0.011 7 Normalized frequency of C-terminal beta-sheet (Chou-Fasman 1978b)
-0.010 9 Normalized frequency of extended structure (Tanaka-Scheraga 1977)
-0.011 9 Hydrophilicity scale (Kuhn et al. 1995)
-0.011 7 Normalized frequency of turn in all-beta class (Palau et al. 1981)
-0.009 9 Relative preference value at N2 (Richardson-Richardson 1988)
-0.013 7 Relative preference value at N" (Richardson-Richardson 1988)
-0.011 9 Normalized positional residue frequency at helix termini N4'(Aurora-Rose
-0.013 9 Average reduced distance for C-alpha (Meirovitch et al. 1980)
-0.016 9 Normalized positional residue frequency at helix termini N'(Aurora-Rose
-0.015 7 Relative preference value at C1 (Richardson-Richardson 1988)
-0.012 9 Normalized hydrophobicity scales for beta-proteins (Cid et al. 1992)
-0.016 9 Average relative fractional occurrence in A0(i-1) (Rackovsky-Scheraga 1982)
-0.015 7 The number of atoms in the side chain labelled 1+1 (Charton-Charton 1983)
-0.016 7 Normalized frequency of C-terminal non beta region (Chou-Fasman 1978b)
-0.014 9 Normalized frequency of N-terminal helix (Chou-Fasman 1978b)
-0.015 9 Average relative fractional occurrence in EL(i-1) (Rackovsky-Scheraga 1982)
-0.016 7 Relative frequency in beta-sheet (Prabhakaran 1990)
-0.016 9 Normalized frequency of zeta R (Maxfield-Scheraga 1976)
-0.018 7 Normalized positional residue frequency at helix termini N3 (Aurora-Rose
-0.018 9 Net charge (Klein et al. 1984)
-0.020 7 Relative preference value at C4 (Richardson-Richardson 1988)
-0.020 9 Aperiodic indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.024 7 Bitterness (Venanzi 1984)
-0.023 9 Normalized relative frequency of extended structure (Isogai et al. 1980)
-0.022 9 Ratio of average and computed composition (Nakashima et al. 1990)
-0.022 9 Beta-strand indices for beta-proteins (Geisow-Roberts 1980)
-0.021 9 Normalized positional residue frequency at helix termini C4' (Aurora-Rose
-0.022 7 Averaged turn propensities in a transmembrane helix (Monne et al. 1999)
-0.018 9 Relative preference value at N3 (Richardson-Richardson 1988)
-0.024 7 Normalized relative frequency of bend (Isogai et al. 1980)
-0.023 9 Relative preference value at N' (Richardson-Richardson 1988)
-0.026 7 Membrane preference for cytochrome b: MPH89 (Degli Esposti et al. 1990)
-0.025 9 Relative frequency in reverse-turn (Prabhakaran 1990)
-0.025 9 SD of AA composition of total proteins (Nakashima et al. 1990)
-0.025 7 Optimized transfer energy parameter (Oobatake et al. 1985)
-0.027 9 Normalized frequency of isolated helix (Tanaka-Scheraga 1977)
-0.028 9 Normalized hydrophobicity scales for alpha/beta-proteins (Cid et al. 1992)
-0.027 7 Normalized frequency of beta-sheet with weights (Levitt 1978)
-0.028 9 Normalized frequency of coil (Tanaka-Scheraga 1977)
-0.028 7 Normalized frequency of coil (Nagano 1973)
-0.029 9 Beta-strand indices (Geisow-Roberts 1980)
-0.029 7 Weights for coil at the window position of 0 (Qian-Sejnowski 1988)
-0.026 9 Free energies of transfer of AcWl-X-LL peptides from bilayer interface to
-0.032 7 Hydrophobicity index (Argos et al. 1982)
-0.032 9 Optimal matching hydrophobicity (Sweet-Eisenberg 1983)
-0.032 7 Average membrane preference: AMP07 (Degli Esposti et al. 1990)
-0.034 9 Relative preference value at N" (Richardson-Richardson 1988)
-0.034 9 Aperiodic indices for beta-proteins (Geisow-Roberts 1980)
-0.033 7 Activation Gibbs energy of unfolding pH7.0 (Yutani et al. 1987)
-0.035 7 Normalized frequency of beta-sheet from CF (Palau et al. 1981)
-0.036 9 Normalized frequency of beta-sheet (Crawford et al. 1973)
-0.036 7 Aperiodic indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.036 9 Relative preference value at C2 (Richardson-Richardson 1988)
-0.037 9 Normalized frequency of beta-sheet from LG (Palau et al. 1981)
-0.037 9 Average relative fractional occurrence in AL(i) (Rackovsky-Scheraga 1982)
-0.038 7 Normalized frequency of bata-structure (Nagano 1973)
-0.038 9 Zimm-Bragg parameter s at 20 C (Sueki et al. 1984)
-0.038 9 Normalized frequency of beta-sheet in all-beta class (Palau et al. 1981)
-0.040 9 Normalized positional residue frequency at helix termini N"' (Aurora-Rose
-0.039 7 Average reduced distance for side chain (Rackovsky-Scheraga 1977)
-0.040 9 Average relative fractional occurrence in ER(i) (Rackovsky-Scheraga 1982)
-0.040 9 Free energy in beta-strand conformation (Munoz-Serrano 1994)
-0.040 7 Beta-strand indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.041 9 Average membrane preference: AMP07 (Degli Esposti et al. 1990)
-0.042 7 Conformational preference for parallel beta-strands (Lifson-Sander 1979)
-0.040 9 Activation Gibbs energy of unfolding pH9.0 (Yutani et al. 1987)
-0.043 9 Average relative fractional occurrence in A0(i) (Rackovsky-Scheraga 1982)
-0.043 9 Normalized frequency of N-terminal beta-sheet (Chou-Fasman 1978b)
-0.042 7 8 A contact number (Nishikawa-Ooi 1980)
-0.044 9 Normalized frequency of zeta L (Maxfield-Scheraga 1976)
-0.046 7 Transfer free energy (Simon 1976) Cited by Charton-Charton (1982)
-0.046 9 AA composition of EXT of multi-spanning proteins (Nakashima-Nishikawa 1992)
-0.046 9 Turn propensity scale for transmembrane helices (Monne et al. 1999)
-0.045 7 Normalized frequency of the 2nd and 3rd residues in turn (Chou-Fasman 1978b)
-0.048 7 Normalized hydrophobicity scales for alpha/beta-proteins (Cid et al. 1992)
-0.047 9 Relative preference value at C1 (Richardson-Richardson 1988)
-0.048 9 Membrane preference for cytochrome b: MPH89 (Degli Esposti et al. 1990)
-0.048 7 Normalized frequency of beta-sheet (Chou-Fasman 1978b)
-0.047 9 Normalized frequency of beta-sheet unweighted (Levitt 1978)
-0.047 7 Ratio of average and computed composition (Nakashima et al. 1990)
-0.049 9 Normalized composition of mt-proteins (Nakashima et al. 1990)
-0.050 7 Average reduced distance for side chain (Meirovitch et al. 1980)
-0.056 9 Normalized average hydrophobicity scales (Cid et al. 1992)
-0.056 7 Average relative probability of inner beta-sheet (Kanehisa-Tsong 1980)
-0.058 9 Relative preference value at C4 (Richardson-Richardson 1988)
-0.058 7 Size (Dawson 1972)
-0.057 9 Conformational preference for antiparallel beta-strands (Lifson-Sander 1979)
-0.057 7 Flexibility parameter for one rigid neighbor (Karplus-Schulz 1985)
-0.056 9 Atom-based hydrophobic moment (Eisenberg-McLachlan 1986)
-0.061 7 Relative preference value at N4 (Richardson-Richardson 1988)
-0.062 9 Distance between C-alpha and centroid of side chain (Levitt 1976)
-0.062 9 Flexibility parameter for one rigid neighbor (Karplus-Schulz 1985)
-0.063 7 Average relative probability of beta-sheet (Kanehisa-Tsong 1980)
-0.064 7 Relative preference value at C3 (Richardson-Richardson 1988)
-0.063 9 Delta G values for the peptides extrapolated to 0 M urea (O'Neil-DeGrado
-0.064 9 Average reduced distance for side chain (Rackovsky-Scheraga 1977)
-0.065 9 Amphiphilicity index (Mitaku et al. 2002)
-0.067 7 Conformational preference for all beta-strands (Lifson-Sander 1979)
-0.070 9 Average reduced distance for side chain (Meirovitch et al. 1980)
-0.069 7 Membrane-buried preference parameters (Argos et al. 1982)
-0.069 9 Spin-spin coupling constants 3JHalpha-NH (Bundi-Wuthrich 1979)
-0.071 9 Hydrophobicity index (Argos et al. 1982)
-0.070 7 Hydrophobicity (Zimmerman et al. 1968)
-0.072 9 Normalized frequency of beta-sheet in alpha/beta class (Palau et al. 1981)
-0.072 7 Number of hydrogen bond donors (Fauchere et al. 1988)
-0.071 9 Optimized propensity to form reverse turn (Oobatake et al. 1985)
-0.073 7 Normalized flexibility parameters (B-values) average (Vihinen et al. 1994)
-0.074 9 Normalized frequency of bata-structure (Nagano 1973)
-0.073 9 Amino acid distribution (Jukes et al. 1975)
-0.076 9 Free energy of solution in water kcal/mole (Charton-Charton 1982)
-0.075 7 Optimized beta-structure-coil equilibrium constant (Oobatake et al. 1985)
-0.078 7 Normalized flexibility parameters (B-values) for each residue surrounded by
-0.077 9 Normalized flexibility parameters (B-values) average (Vihinen et al. 1994)
-0.079 9 Normalized frequency of beta-sheet (Chou-Fasman 1978b)
-0.078 7 Solvation free energy (Eisenberg-McLachlan 1986)
-0.079 9 pK-a(RCOOH) (Fauchere et al. 1988)
-0.082 9 Partition coefficient (Pliska et al. 1981)
-0.081 7 Transfer energy organic solvent/water (Nozaki-Tanford 1971)
-0.082 9 Normalized positional residue frequency at helix termini C"' (Aurora-Rose
-0.083 7 Principal property value z3 (Wold et al. 1987)
-0.083 9 Optimized transfer energy parameter (Oobatake et al. 1985)
-0.085 9 Normalized flexibility parameters (B-values) for each residue surrounded by
-0.085 7 Signal sequence helical potential (Argos et al. 1982)
-0.088 7 Activation Gibbs energy of unfolding pH9.0 (Yutani et al. 1987)
-0.089 9 Transfer free energy (Simon 1976) Cited by Charton-Charton (1982)
-0.091 9 Averaged turn propensities in a transmembrane helix (Monne et al. 1999)
-0.090 7 Hydrophobicity (Jones 1975)
-0.092 9 Number of hydrogen bond donors (Fauchere et al. 1988)
-0.094 7 Graph shape index (Fauchere et al. 1988)
-0.095 9 Relative preference value at N4 (Richardson-Richardson 1988)
-0.097 7 Normalized hydrophobicity scales for beta-proteins (Cid et al. 1992)
-0.099 9 Hydrophobicity factor (Goldsack-Chalifoux 1973)
-0.100 7 Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/2-PrOH/MeCN/H2O
-0.100 9 STERIMOL maximum width of the side chain (Fauchere et al. 1988)
-0.100 7 Mean polarity (Radzicka-Wolfenden 1988)
-0.103 9 STERIMOL length of the side chain (Fauchere et al. 1988)
-0.103 7 Partition coefficient (Pliska et al. 1981)
-0.106 7 Normalized average hydrophobicity scales (Cid et al. 1992)
-0.109 7 Principal property value z2 (Wold et al. 1987)
-0.109 9 Hydration number (Hopfinger 1971) Cited by Charton-Charton (1982)
-0.111 7 Hydrophobic parameter pi (Fauchere-Pliska 1983)
-0.113 9 Conformational preference for parallel beta-strands (Lifson-Sander 1979)
-0.113 9 Isoelectric point (Zimmerman et al. 1968)
-0.113 7 Transfer free energy to surface (Bull-Breese 1974)
-0.118 9 Normalized composition from animal (Nakashima et al. 1990)
-0.121 7 Average number of surrounding residues (Ponnuswamy et al. 1980)
-0.121 9 Hydrophobicity (Zimmerman et al. 1968)
-0.124 9 Principal property value z2 (Wold et al. 1987)
-0.124 7 Normalized hydrophobicity scales for alpha+beta-proteins (Cid et al. 1992)
-0.127 9 Number of full nonbonding orbitals (Fauchere et al. 1988)
-0.128 7 Partition energy (Guy 1985)
-0.130 7 van der Waals parameter R0 (Levitt 1976)
-0.131 9 Side chain orientational preference (Rackovsky-Scheraga 1977)
-0.132 7 Ratio of buried and accessible molar fractions (Janin 1979)
-0.132 9 AA composition of EXT of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.135 9 Hydrophobicity (Jones 1975)
-0.135 7 Hydration number (Hopfinger 1971) Cited by Charton-Charton (1982)
-0.136 9 Optimized beta-structure-coil equilibrium constant (Oobatake et al. 1985)
-0.138 7 Transfer free energy from vap to chx (Radzicka-Wolfenden 1988)
-0.144 7 Polarity (Zimmerman et al. 1968)
-0.147 9 Hydrophilicity value (Hopp-Woods 1981)
-0.148 7 Transfer free energy from oct to wat (Radzicka-Wolfenden 1988)
-0.151 9 Composition of amino acids in anchored proteins (percent) (Cedano et al.
-0.154 7 The number of bonds in the longest chain (Charton-Charton 1983)
-0.156 9 Normalized hydrophobicity scales for alpha+beta-proteins (Cid et al. 1992)
-0.156 7 Number of full nonbonding orbitals (Fauchere et al. 1988)
-0.157 9 The number of bonds in the longest chain (Charton-Charton 1983)
-0.159 7 Beta-coil equilibrium constant (Ptitsyn-Finkelstein 1983)
-0.158 9 Graph shape index (Fauchere et al. 1988)
-0.163 7 Side chain orientational preference (Rackovsky-Scheraga 1977)
-0.163 9 van der Waals parameter R0 (Levitt 1976)
-0.166 9 Size (Dawson 1972)
-0.165 7 Normalized composition from animal (Nakashima et al. 1990)
-0.168 9 Surrounding hydrophobicity in alpha-helix (Ponnuswamy et al. 1980)
-0.168 7 Effective partition energy (Miyazawa-Jernigan 1985)
-0.170 9 Average number of surrounding residues (Ponnuswamy et al. 1980)
-0.172 7 STERIMOL length of the side chain (Fauchere et al. 1988)
-0.174 9 Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/2-PrOH/MeCN/H2O
-0.175 9 Hydrophobic parameter (Levitt 1976)
-0.176 7 Surrounding hydrophobicity in beta-sheet (Ponnuswamy et al. 1980)
-0.180 7 Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/MeCN/H2O (Wilce et
-0.180 9 Principal property value z3 (Wold et al. 1987)
-0.181 9 Effective partition energy (Miyazawa-Jernigan 1985)
-0.182 7 Hydrophilicity value (Hopp-Woods 1981)
-0.183 9 Normalized van der Waals volume (Fauchere et al. 1988)
-0.185 7 Surrounding hydrophobicity in alpha-helix (Ponnuswamy et al. 1980)
-0.186 9 Surrounding hydrophobicity in beta-sheet (Ponnuswamy et al. 1980)
-0.190 9 Composition of amino acids in extracellular proteins (percent) (Cedano et