*** mRMR features ***
ScorePosition Name
0.3199Hydropathy scale based on self-information values in the two-state model
0.0337Normalized frequency of beta-turn (Chou-Fasman 1978b)
0.0247alpha-CH chemical shifts (Andersen et al. 1992)
0.0097Hydrophobicity factor (Goldsack-Chalifoux 1973)
0.0299Negative charge (Fauchere et al. 1988)
-0.0107Relative preference value at N' (Richardson-Richardson 1988)
0.0029Loss of Side chain hydropathy by helix formation (Roseman 1988)
-0.0087Normalized frequency of beta-sheet unweighted (Levitt 1978)
-0.0099Helix termination parameter at posision j+1 (Finkelstein et al. 1991)
-0.0137Normalized frequency of N-terminal non beta region (Chou-Fasman 1978b)
-0.0149A parameter of charge transfer capability (Charton-Charton 1983)
-0.0199Linker propensity from long dataset (linker length is greater than 14
-0.0177The Chou-Fasman parameter of the coil conformation (Charton-Charton 1983)
-0.0147Propensity of amino acids within pi-helices (Fodje-Al-Karadaghi 2002)
0.0029Normalized composition from fungi and plant (Nakashima et al. 1990)
-0.0199Helix termination parameter at posision j-2j-1j (Finkelstein et al. 1991)
-0.0169Relative preference value at Mid (Richardson-Richardson 1988)
-0.0177Normalized frequency of chain reversal D (Tanaka-Scheraga 1977)
-0.0129Normalized relative frequency of double bend (Isogai et al. 1980)
-0.0157Turn propensity scale for transmembrane helices (Monne et al. 1999)
-0.0099Relative preference value at N1 (Richardson-Richardson 1988)
-0.0209Linker propensity from small dataset (linker length is less than six
-0.0217Normalized frequency of beta-sheet (Crawford et al. 1973)
-0.0179Normalized positional residue frequency at helix termini N2 (Aurora-Rose
-0.0227Normalized frequency of beta-sheet in alpha/beta class (Palau et al. 1981)
-0.0199Linker propensity from 3-linker dataset (George-Heringa 2003)
-0.0159Linker propensity from 1-linker dataset (George-Heringa 2003)
-0.0159Average relative fractional occurrence in E0(i-1) (Rackovsky-Scheraga 1982)
-0.0167Hydrophilicity scale (Kuhn et al. 1995)
-0.0119Normalized positional residue frequency at helix termini N" (Aurora-Rose
-0.0129Normalized positional residue frequency at helix termini N1 (Aurora-Rose
-0.0147Normalized positional residue frequency at helix termini N"' (Aurora-Rose
-0.0179Average relative fractional occurrence in EL(i) (Rackovsky-Scheraga 1982)
-0.0179Normalized frequency of N-terminal non helical region (Chou-Fasman 1978b)
-0.0157Average gain ratio in surrounding hydrophobicity (Ponnuswamy et al. 1980)
-0.0139The number of atoms in the side chain labelled 3+1 (Charton-Charton 1983)
-0.0149Relative preference value at N5 (Richardson-Richardson 1988)
-0.0147Normalized frequency of chain reversal (Tanaka-Scheraga 1977)
-0.0119Normalized frequency of reverse turn unweighted (Levitt 1978)
-0.0139Linker propensity from 2-linker dataset (George-Heringa 2003)
-0.0117Normalized frequency of C-terminal beta-sheet (Chou-Fasman 1978b)
-0.0109Normalized frequency of extended structure (Tanaka-Scheraga 1977)
-0.0119Hydrophilicity scale (Kuhn et al. 1995)
-0.0117Normalized frequency of turn in all-beta class (Palau et al. 1981)
-0.0099Relative preference value at N2 (Richardson-Richardson 1988)
-0.0137Relative preference value at N" (Richardson-Richardson 1988)
-0.0119Normalized positional residue frequency at helix termini N4'(Aurora-Rose
-0.0139Average reduced distance for C-alpha (Meirovitch et al. 1980)
-0.0169Normalized positional residue frequency at helix termini N'(Aurora-Rose
-0.0157Relative preference value at C1 (Richardson-Richardson 1988)
-0.0129Normalized hydrophobicity scales for beta-proteins (Cid et al. 1992)
-0.0169Average relative fractional occurrence in A0(i-1) (Rackovsky-Scheraga 1982)
-0.0157The number of atoms in the side chain labelled 1+1 (Charton-Charton 1983)
-0.0167Normalized frequency of C-terminal non beta region (Chou-Fasman 1978b)
-0.0149Normalized frequency of N-terminal helix (Chou-Fasman 1978b)
-0.0159Average relative fractional occurrence in EL(i-1) (Rackovsky-Scheraga 1982)
-0.0167Relative frequency in beta-sheet (Prabhakaran 1990)
-0.0169Normalized frequency of zeta R (Maxfield-Scheraga 1976)
-0.0187Normalized positional residue frequency at helix termini N3 (Aurora-Rose
-0.0189Net charge (Klein et al. 1984)
-0.0207Relative preference value at C4 (Richardson-Richardson 1988)
-0.0209Aperiodic indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.0247Bitterness (Venanzi 1984)
-0.0239Normalized relative frequency of extended structure (Isogai et al. 1980)
-0.0229Ratio of average and computed composition (Nakashima et al. 1990)
-0.0229Beta-strand indices for beta-proteins (Geisow-Roberts 1980)
-0.0219Normalized positional residue frequency at helix termini C4' (Aurora-Rose
-0.0227Averaged turn propensities in a transmembrane helix (Monne et al. 1999)
-0.0189Relative preference value at N3 (Richardson-Richardson 1988)
-0.0247Normalized relative frequency of bend (Isogai et al. 1980)
-0.0239Relative preference value at N' (Richardson-Richardson 1988)
-0.0267Membrane preference for cytochrome b: MPH89 (Degli Esposti et al. 1990)
-0.0259Relative frequency in reverse-turn (Prabhakaran 1990)
-0.0259SD of AA composition of total proteins (Nakashima et al. 1990)
-0.0257Optimized transfer energy parameter (Oobatake et al. 1985)
-0.0279Normalized frequency of isolated helix (Tanaka-Scheraga 1977)
-0.0289Normalized hydrophobicity scales for alpha/beta-proteins (Cid et al. 1992)
-0.0277Normalized frequency of beta-sheet with weights (Levitt 1978)
-0.0289Normalized frequency of coil (Tanaka-Scheraga 1977)
-0.0287Normalized frequency of coil (Nagano 1973)
-0.0299Beta-strand indices (Geisow-Roberts 1980)
-0.0297Weights for coil at the window position of 0 (Qian-Sejnowski 1988)
-0.0269Free energies of transfer of AcWl-X-LL peptides from bilayer interface to
-0.0327Hydrophobicity index (Argos et al. 1982)
-0.0329Optimal matching hydrophobicity (Sweet-Eisenberg 1983)
-0.0327Average membrane preference: AMP07 (Degli Esposti et al. 1990)
-0.0349Relative preference value at N" (Richardson-Richardson 1988)
-0.0349Aperiodic indices for beta-proteins (Geisow-Roberts 1980)
-0.0337Activation Gibbs energy of unfolding pH7.0 (Yutani et al. 1987)
-0.0357Normalized frequency of beta-sheet from CF (Palau et al. 1981)
-0.0369Normalized frequency of beta-sheet (Crawford et al. 1973)
-0.0367Aperiodic indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.0369Relative preference value at C2 (Richardson-Richardson 1988)
-0.0379Normalized frequency of beta-sheet from LG (Palau et al. 1981)
-0.0379Average relative fractional occurrence in AL(i) (Rackovsky-Scheraga 1982)
-0.0387Normalized frequency of bata-structure (Nagano 1973)
-0.0389Zimm-Bragg parameter s at 20 C (Sueki et al. 1984)
-0.0389Normalized frequency of beta-sheet in all-beta class (Palau et al. 1981)
-0.0409Normalized positional residue frequency at helix termini N"' (Aurora-Rose
-0.0397Average reduced distance for side chain (Rackovsky-Scheraga 1977)
-0.0409Average relative fractional occurrence in ER(i) (Rackovsky-Scheraga 1982)
-0.0409Free energy in beta-strand conformation (Munoz-Serrano 1994)
-0.0407Beta-strand indices for alpha/beta-proteins (Geisow-Roberts 1980)
-0.0419Average membrane preference: AMP07 (Degli Esposti et al. 1990)
-0.0427Conformational preference for parallel beta-strands (Lifson-Sander 1979)
-0.0409Activation Gibbs energy of unfolding pH9.0 (Yutani et al. 1987)
-0.0439Average relative fractional occurrence in A0(i) (Rackovsky-Scheraga 1982)
-0.0439Normalized frequency of N-terminal beta-sheet (Chou-Fasman 1978b)
-0.04278 A contact number (Nishikawa-Ooi 1980)
-0.0449Normalized frequency of zeta L (Maxfield-Scheraga 1976)
-0.0467Transfer free energy (Simon 1976) Cited by Charton-Charton (1982)
-0.0469AA composition of EXT of multi-spanning proteins (Nakashima-Nishikawa 1992)
-0.0469Turn propensity scale for transmembrane helices (Monne et al. 1999)
-0.0457Normalized frequency of the 2nd and 3rd residues in turn (Chou-Fasman 1978b)
-0.0487Normalized hydrophobicity scales for alpha/beta-proteins (Cid et al. 1992)
-0.0479Relative preference value at C1 (Richardson-Richardson 1988)
-0.0489Membrane preference for cytochrome b: MPH89 (Degli Esposti et al. 1990)
-0.0487Normalized frequency of beta-sheet (Chou-Fasman 1978b)
-0.0479Normalized frequency of beta-sheet unweighted (Levitt 1978)
-0.0477Ratio of average and computed composition (Nakashima et al. 1990)
-0.0499Normalized composition of mt-proteins (Nakashima et al. 1990)
-0.0507Average reduced distance for side chain (Meirovitch et al. 1980)
-0.0569Normalized average hydrophobicity scales (Cid et al. 1992)
-0.0567Average relative probability of inner beta-sheet (Kanehisa-Tsong 1980)
-0.0589Relative preference value at C4 (Richardson-Richardson 1988)
-0.0587Size (Dawson 1972)
-0.0579Conformational preference for antiparallel beta-strands (Lifson-Sander 1979)
-0.0577Flexibility parameter for one rigid neighbor (Karplus-Schulz 1985)
-0.0569Atom-based hydrophobic moment (Eisenberg-McLachlan 1986)
-0.0617Relative preference value at N4 (Richardson-Richardson 1988)
-0.0629Distance between C-alpha and centroid of side chain (Levitt 1976)
-0.0629Flexibility parameter for one rigid neighbor (Karplus-Schulz 1985)
-0.0637Average relative probability of beta-sheet (Kanehisa-Tsong 1980)
-0.0647Relative preference value at C3 (Richardson-Richardson 1988)
-0.0639Delta G values for the peptides extrapolated to 0 M urea (O'Neil-DeGrado
-0.0649Average reduced distance for side chain (Rackovsky-Scheraga 1977)
-0.0659Amphiphilicity index (Mitaku et al. 2002)
-0.0677Conformational preference for all beta-strands (Lifson-Sander 1979)
-0.0709Average reduced distance for side chain (Meirovitch et al. 1980)
-0.0697Membrane-buried preference parameters (Argos et al. 1982)
-0.0699Spin-spin coupling constants 3JHalpha-NH (Bundi-Wuthrich 1979)
-0.0719Hydrophobicity index (Argos et al. 1982)
-0.0707Hydrophobicity (Zimmerman et al. 1968)
-0.0729Normalized frequency of beta-sheet in alpha/beta class (Palau et al. 1981)
-0.0727Number of hydrogen bond donors (Fauchere et al. 1988)
-0.0719Optimized propensity to form reverse turn (Oobatake et al. 1985)
-0.0737Normalized flexibility parameters (B-values) average (Vihinen et al. 1994)
-0.0749Normalized frequency of bata-structure (Nagano 1973)
-0.0739Amino acid distribution (Jukes et al. 1975)
-0.0769Free energy of solution in water kcal/mole (Charton-Charton 1982)
-0.0757Optimized beta-structure-coil equilibrium constant (Oobatake et al. 1985)
-0.0787Normalized flexibility parameters (B-values) for each residue surrounded by
-0.0779Normalized flexibility parameters (B-values) average (Vihinen et al. 1994)
-0.0799Normalized frequency of beta-sheet (Chou-Fasman 1978b)
-0.0787Solvation free energy (Eisenberg-McLachlan 1986)
-0.0799pK-a(RCOOH) (Fauchere et al. 1988)
-0.0829Partition coefficient (Pliska et al. 1981)
-0.0817Transfer energy organic solvent/water (Nozaki-Tanford 1971)
-0.0829Normalized positional residue frequency at helix termini C"' (Aurora-Rose
-0.0837Principal property value z3 (Wold et al. 1987)
-0.0839Optimized transfer energy parameter (Oobatake et al. 1985)
-0.0859Normalized flexibility parameters (B-values) for each residue surrounded by
-0.0857Signal sequence helical potential (Argos et al. 1982)
-0.0887Activation Gibbs energy of unfolding pH9.0 (Yutani et al. 1987)
-0.0899Transfer free energy (Simon 1976) Cited by Charton-Charton (1982)
-0.0919Averaged turn propensities in a transmembrane helix (Monne et al. 1999)
-0.0907Hydrophobicity (Jones 1975)
-0.0929Number of hydrogen bond donors (Fauchere et al. 1988)
-0.0947Graph shape index (Fauchere et al. 1988)
-0.0959Relative preference value at N4 (Richardson-Richardson 1988)
-0.0977Normalized hydrophobicity scales for beta-proteins (Cid et al. 1992)
-0.0999Hydrophobicity factor (Goldsack-Chalifoux 1973)
-0.1007Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/2-PrOH/MeCN/H2O
-0.1009STERIMOL maximum width of the side chain (Fauchere et al. 1988)
-0.1007Mean polarity (Radzicka-Wolfenden 1988)
-0.1039STERIMOL length of the side chain (Fauchere et al. 1988)
-0.1037Partition coefficient (Pliska et al. 1981)
-0.1067Normalized average hydrophobicity scales (Cid et al. 1992)
-0.1097Principal property value z2 (Wold et al. 1987)
-0.1099Hydration number (Hopfinger 1971) Cited by Charton-Charton (1982)
-0.1117Hydrophobic parameter pi (Fauchere-Pliska 1983)
-0.1139Conformational preference for parallel beta-strands (Lifson-Sander 1979)
-0.1139Isoelectric point (Zimmerman et al. 1968)
-0.1137Transfer free energy to surface (Bull-Breese 1974)
-0.1189Normalized composition from animal (Nakashima et al. 1990)
-0.1217Average number of surrounding residues (Ponnuswamy et al. 1980)
-0.1219Hydrophobicity (Zimmerman et al. 1968)
-0.1249Principal property value z2 (Wold et al. 1987)
-0.1247Normalized hydrophobicity scales for alpha+beta-proteins (Cid et al. 1992)
-0.1279Number of full nonbonding orbitals (Fauchere et al. 1988)
-0.1287Partition energy (Guy 1985)
-0.1307van der Waals parameter R0 (Levitt 1976)
-0.1319Side chain orientational preference (Rackovsky-Scheraga 1977)
-0.1327Ratio of buried and accessible molar fractions (Janin 1979)
-0.1329AA composition of EXT of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.1359Hydrophobicity (Jones 1975)
-0.1357Hydration number (Hopfinger 1971) Cited by Charton-Charton (1982)
-0.1369Optimized beta-structure-coil equilibrium constant (Oobatake et al. 1985)
-0.1387Transfer free energy from vap to chx (Radzicka-Wolfenden 1988)
-0.1447Polarity (Zimmerman et al. 1968)
-0.1479Hydrophilicity value (Hopp-Woods 1981)
-0.1487Transfer free energy from oct to wat (Radzicka-Wolfenden 1988)
-0.1519Composition of amino acids in anchored proteins (percent) (Cedano et al.
-0.1547The number of bonds in the longest chain (Charton-Charton 1983)
-0.1569Normalized hydrophobicity scales for alpha+beta-proteins (Cid et al. 1992)
-0.1567Number of full nonbonding orbitals (Fauchere et al. 1988)
-0.1579The number of bonds in the longest chain (Charton-Charton 1983)
-0.1597Beta-coil equilibrium constant (Ptitsyn-Finkelstein 1983)
-0.1589Graph shape index (Fauchere et al. 1988)
-0.1637Side chain orientational preference (Rackovsky-Scheraga 1977)
-0.1639van der Waals parameter R0 (Levitt 1976)
-0.1669Size (Dawson 1972)
-0.1657Normalized composition from animal (Nakashima et al. 1990)
-0.1689Surrounding hydrophobicity in alpha-helix (Ponnuswamy et al. 1980)
-0.1687Effective partition energy (Miyazawa-Jernigan 1985)
-0.1709Average number of surrounding residues (Ponnuswamy et al. 1980)
-0.1727STERIMOL length of the side chain (Fauchere et al. 1988)
-0.1749Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/2-PrOH/MeCN/H2O
-0.1759Hydrophobic parameter (Levitt 1976)
-0.1767Surrounding hydrophobicity in beta-sheet (Ponnuswamy et al. 1980)
-0.1807Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/MeCN/H2O (Wilce et
-0.1809Principal property value z3 (Wold et al. 1987)
-0.1819Effective partition energy (Miyazawa-Jernigan 1985)
-0.1827Hydrophilicity value (Hopp-Woods 1981)
-0.1839Normalized van der Waals volume (Fauchere et al. 1988)
-0.1857Surrounding hydrophobicity in alpha-helix (Ponnuswamy et al. 1980)
-0.1869Surrounding hydrophobicity in beta-sheet (Ponnuswamy et al. 1980)
-0.1909Composition of amino acids in extracellular proteins (percent) (Cedano et
-0.1917Hydration free energy (Robson-Osguthorpe 1979)
-0.1949Polarity (Zimmerman et al. 1968)
-0.1967The relative stability scale extracted from mutation experiments (Zhou-Zhou
-0.1979Information measure for extended without H-bond (Robson-Suzuki 1976)
-0.1997Hydrophobicity scales (Ponnuswamy 1993)
-0.1989Ratio of buried and accessible molar fractions (Janin 1979)
-0.2027Hydrophobic parameter (Levitt 1976)
-0.2019Partition energy (Guy 1985)
-0.2049Transfer free energy from vap to chx (Radzicka-Wolfenden 1988)
-0.2067Distribution of amino acid residues in the alpha-helices in mesophilic
-0.2099Solvation free energy (Eisenberg-McLachlan 1986)
-0.2097Average surrounding hydrophobicity (Manavalan-Ponnuswamy 1978)
-0.2129Beta-coil equilibrium constant (Ptitsyn-Finkelstein 1983)
-0.2167Normalized van der Waals volume (Fauchere et al. 1988)
-0.2159Distribution of amino acid residues in the alpha-helices in mesophilic
-0.2189Hydration free energy (Robson-Osguthorpe 1979)
-0.2229AA composition of CYT of multi-spanning proteins (Nakashima-Nishikawa 1992)
-0.2217The stability scale from the knowledge-based atom-atom potential (Zhou-Zhou
-0.2269AA composition of CYT of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.2267Accessibility reduction ratio (Ponnuswamy et al. 1980)
-0.2299The relative stability scale extracted from mutation experiments (Zhou-Zhou
-0.2317Side chain angle theta(AAR) (Levitt 1976)
-0.2399The stability scale from the knowledge-based atom-atom potential (Zhou-Zhou
-0.2417Information measure for extended without H-bond (Robson-Suzuki 1976)
-0.2409Entire chain compositino of amino acids in nuclear proteins (percent)
-0.2467Surrounding hydrophobicity in turn (Ponnuswamy et al. 1980)
-0.2469Hydrophobicity scales (Ponnuswamy 1993)
-0.2499Entire chain composition of amino acids in extracellular proteins of
-0.2507AA composition of CYT of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.2539Amino acid composition (Dayhoff et al. 1978a)
-0.2577Entire chain composition of amino acids in extracellular proteins of
-0.2579Entire chain composition of amino acids in intracellular proteins of
-0.2607Surrounding hydrophobicity in folded form (Ponnuswamy et al. 1980)
-0.2629Accessibility reduction ratio (Ponnuswamy et al. 1980)
-0.2669Side chain angle theta(AAR) (Levitt 1976)
-0.2697Average interactions per side chain atom (Warme-Morgan 1978)
-0.2747Entire chain composition of amino acids in intracellular proteins of
-0.2749Surrounding hydrophobicity in turn (Ponnuswamy et al. 1980)
-0.2779Hydrophobicity coefficient in RP-HPLC C18 with 0.1%TFA/MeCN/H2O (Wilce et
-0.2797Interior composition of amino acids in extracellular proteins of mesophiles
-0.2819Unfolding Gibbs energy in water pH9.0 (Yutani et al. 1987)
-0.2847Composition of amino acids in nuclear proteins (percent) (Cedano et al.
-0.2879Distribution of amino acid residues in the alpha-helices in thermophilic
-0.2897Interior composition of amino acids in intracellular proteins of mesophiles
-0.2939Average surrounding hydrophobicity (Manavalan-Ponnuswamy 1978)
-0.2937Average gain in surrounding hydrophobicity (Ponnuswamy et al. 1980)
-0.2949Composition of amino acids in nuclear proteins (percent) (Cedano et al.
-0.2977Side chain interaction parameter (Krigbaum-Komoriya 1979)
-0.2989Short and medium range non-bonded energy per residue (Oobatake-Ooi 1977)
-0.3037N.m.r. chemical shift of alpha-carbon (Fauchere et al. 1988)
-0.3029Composition of amino acids in intracellular proteins (percent) (Cedano et
-0.3059Average interactions per side chain atom (Warme-Morgan 1978)
-0.3107Side chain hydropathy corrected for solvation (Roseman 1988)
-0.3099AA composition of total proteins (Nakashima et al. 1990)
-0.3139Surrounding hydrophobicity in folded form (Ponnuswamy et al. 1980)
-0.3137Principal property value z1 (Wold et al. 1987)
-0.3177Information measure for coil (Robson-Suzuki 1976)
-0.3179N.m.r. chemical shift of alpha-carbon (Fauchere et al. 1988)
-0.3217Transfer free energy from vap to oct (Radzicka-Wolfenden 1988)
-0.3209Principal property value z1 (Wold et al. 1987)
-0.3247Information measure for N-terminal turn (Robson-Suzuki 1976)
-0.3239Side chain hydropathy corrected for solvation (Roseman 1988)
-0.3289Information measure for C-terminal turn (Robson-Suzuki 1976)
-0.3277AA composition of membrane proteins (Nakashima et al. 1990)
-0.3319Hydrophobicity coefficient in RP-HPLC C4 with 0.1%TFA/MeCN/H2O (Wilce et al.
-0.3317Side chain interaction parameter (Krigbaum-Rubin 1971)
-0.3369AA composition of membrane proteins (Nakashima et al. 1990)
-0.3387AA composition of EXT2 of single-spanning proteins (Nakashima-Nishikawa
-0.3429Side chain interaction parameter (Krigbaum-Komoriya 1979)
-0.3427Composition of amino acids in membrane proteins (percent) (Cedano et al.
-0.3459Average gain in surrounding hydrophobicity (Ponnuswamy et al. 1980)
-0.3457Unfolding Gibbs energy in water pH9.0 (Yutani et al. 1987)
-0.3499Information measure for N-terminal turn (Robson-Suzuki 1976)
-0.3497Hydropathy index (Kyte-Doolittle 1982)
-0.3587Information measure for C-terminal turn (Robson-Suzuki 1976)
-0.3619Information measure for coil (Robson-Suzuki 1976)
-0.3627Distribution of amino acid residues in the alpha-helices in thermophilic
-0.3649Side chain interaction parameter (Krigbaum-Rubin 1971)
-0.3667Information measure for loop (Robson-Suzuki 1976)
-0.3679Surface composition of amino acids in nuclear proteins (percent)
-0.3717Hydrophobicity coefficient in RP-HPLC C4 with 0.1%TFA/MeCN/H2O (Wilce et al.
-0.3709Interior composition of amino acids in intracellular proteins of mesophiles
-0.3747Transmembrane regions of non-mt-proteins (Nakashima et al. 1990)
-0.3749AA composition of EXT2 of single-spanning proteins (Nakashima-Nishikawa
-0.3777Information measure for N-terminal helix (Robson-Suzuki 1976)
-0.3819Surface composition of amino acids in intracellular proteins of thermophiles
-0.3827Information measure for pleated-sheet (Robson-Suzuki 1976)
-0.3859Information measure for pleated-sheet (Robson-Suzuki 1976)
-0.3887Distribution of amino acid residues in the 18 non-redundant families of
-0.3889Transfer free energy from vap to oct (Radzicka-Wolfenden 1988)
-0.3927Interior composition of amino acids in nuclear proteins (percent)
-0.3919Composition of amino acids in membrane proteins (percent) (Cedano et al.
-0.3969Entire chain composition of amino acids in intracellular proteins of
-0.3977Entire chain composition of amino acids in intracellular proteins of
-0.4019Information measure for N-terminal helix (Robson-Suzuki 1976)
-0.4047Information measure for turn (Robson-Suzuki 1976)
-0.4119Polarity (Grantham 1974)
-0.4117Surface composition of amino acids in intracellular proteins of thermophiles
-0.4149Distribution of amino acid residues in the 18 non-redundant families of
-0.4167Distribution of amino acid residues in the 18 non-redundant families of
-0.4189Optimized side chain interaction parameter (Oobatake et al. 1985)
-0.4217Unfolding Gibbs energy in water pH7.0 (Yutani et al. 1987)
-0.4239Information measure for loop (Robson-Suzuki 1976)
-0.4257Optimized side chain interaction parameter (Oobatake et al. 1985)
-0.4279Transmembrane regions of non-mt-proteins (Nakashima et al. 1990)
-0.4287Information measure for middle turn (Robson-Suzuki 1976)
-0.4329Information measure for turn (Robson-Suzuki 1976)
-0.4337Polarity (Grantham 1974)
-0.4369Interior composition of amino acids in extracellular proteins of mesophiles
-0.4377AA composition of mt-proteins (Nakashima et al. 1990)
-0.4389Polar requirement (Woese 1973)
-0.4427Hydrophobicity coefficient in RP-HPLC C8 with 0.1%TFA/MeCN/H2O (Wilce et al.
-0.4429Hydrophobicity coefficient in RP-HPLC C8 with 0.1%TFA/MeCN/H2O (Wilce et al.
-0.4479Surface composition of amino acids in extracellular proteins of mesophiles
-0.4467Interior composition of amino acids in intracellular proteins of thermophiles
-0.4499Distribution of amino acid residues in the 18 non-redundant families of
-0.4517Transmembrane regions of mt-proteins (Nakashima et al. 1990)
-0.4529Transfer free energy from chx to oct (Radzicka-Wolfenden 1988)
-0.4567AA composition of mt-proteins from animal (Nakashima et al. 1990)
-0.455914 A contact number (Nishikawa-Ooi 1986)
-0.4607Surface composition of amino acids in nuclear proteins (percent)
-0.4609AA composition of mt-proteins (Nakashima et al. 1990)
-0.4637AA composition of mt-proteins from fungi and plant (Nakashima et al. 1990)
-0.4629Interior composition of amino acids in intracellular proteins of thermophiles
-0.4669Hydropathy index (Kyte-Doolittle 1982)
-0.4657Surface composition of amino acids in extracellular proteins of mesophiles
-0.4699Zimm-Bragg parameter sigma x 1.0E4 (Sueki et al. 1984)
-0.4707Modified Kyte-Doolittle hydrophobicity scale (Juretic et al. 1998)
-0.4749AA composition of mt-proteins from animal (Nakashima et al. 1990)
-0.4747Polar requirement (Woese 1973)
-0.4779Interior composition of amino acids in nuclear proteins (percent)
-0.4867Transfer free energy from chx to oct (Radzicka-Wolfenden 1988)
-0.4879AA composition of mt-proteins from fungi and plant (Nakashima et al. 1990)
-0.493714 A contact number (Nishikawa-Ooi 1986)
-0.4939Value of theta(i-1) (Rackovsky-Scheraga 1982)
-0.4969Unfolding Gibbs energy in water pH7.0 (Yutani et al. 1987)
-0.4997Hydration potential (Wolfenden et al. 1981)
-0.5019AA composition of CYT2 of single-spanning proteins (Nakashima-Nishikawa
-0.5037Value of theta(i-1) (Rackovsky-Scheraga 1982)
-0.5069Retention coefficient in NaH2PO4 (Meek-Rossetti 1981)
-0.5077Side chain hydropathy uncorrected for solvation (Roseman 1988)
-0.5099Surface composition of amino acids in intracellular proteins of mesophiles
-0.5107Information measure for C-terminal helix (Robson-Suzuki 1976)
-0.5169Hydration potential (Wolfenden et al. 1981)
-0.5187Transfer free energy from chx to wat (Radzicka-Wolfenden 1988)
-0.5199Information measure for middle turn (Robson-Suzuki 1976)
-0.5217Zimm-Bragg parameter sigma x 1.0E4 (Sueki et al. 1984)
-0.5239Information measure for extended (Robson-Suzuki 1976)
-0.5247AA composition of MEM of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.5289Side chain hydropathy uncorrected for solvation (Roseman 1988)
-0.5277RF rank (Zimmerman et al. 1968)
-0.5317Information measure for extended (Robson-Suzuki 1976)
-0.5309Transmembrane regions of mt-proteins (Nakashima et al. 1990)
-0.5357Retention coefficient in NaH2PO4 (Meek-Rossetti 1981)
-0.5339Information measure for middle helix (Robson-Suzuki 1976)
-0.5427Bulkiness (Zimmerman et al. 1968)
-0.5449RF rank (Zimmerman et al. 1968)
-0.5507Retention coefficient in HPLC pH7.4 (Meek 1980)
-0.5499Modified Kyte-Doolittle hydrophobicity scale (Juretic et al. 1998)
-0.5547Information measure for middle helix (Robson-Suzuki 1976)
-0.5549Retention coefficient in HPLC pH7.4 (Meek 1980)
-0.5597AA composition of CYT2 of single-spanning proteins (Nakashima-Nishikawa
-0.5669Average non-bonded energy per residue (Oobatake-Ooi 1977)
-0.5687Surface composition of amino acids in intracellular proteins of mesophiles
-0.5709Bulkiness (Zimmerman et al. 1968)
-0.5759Retention coefficient in HFBA (Browne et al. 1982)
-0.5787Average non-bonded energy per residue (Oobatake-Ooi 1977)
-0.5779AA composition of MEM of single-spanning proteins (Nakashima-Nishikawa 1992)
-0.5837Buriability (Zhou-Zhou 2004)
-0.5849Transfer free energy from chx to wat (Radzicka-Wolfenden 1988)
-0.5889Information measure for C-terminal helix (Robson-Suzuki 1976)
-0.5887AA composition of MEM of multi-spanning proteins (Nakashima-Nishikawa 1992)
-0.5999HPLC parameter (Parker et al. 1986)
-0.5997HPLC parameter (Parker et al. 1986)
-0.6049Value of theta(i) (Rackovsky-Scheraga 1982)
-0.6047Retention coefficient in HFBA (Browne et al. 1982)
-0.6069Buriability (Zhou-Zhou 2004)
-0.6087Retention coefficient in NaClO4 (Meek-Rossetti 1981)
-0.6157Value of theta(i) (Rackovsky-Scheraga 1982)
-0.6199AA composition of MEM of multi-spanning proteins (Nakashima-Nishikawa 1992)
-0.6299Side-chain contribution to protein stability (kJ/mol) (Takano-Yutani 2001)
-0.6339Information measure for alpha-helix (Robson-Suzuki 1976)
-0.6327Side-chain contribution to protein stability (kJ/mol) (Takano-Yutani 2001)
-0.6389Retention coefficient in NaClO4 (Meek-Rossetti 1981)
-0.6539Retention coefficient in HPLC pH2.1 (Meek 1980)
-0.6617Volumes including the crystallographic waters using the ProtOr (Tsai et al.
-0.6747Retention coefficient in HPLC pH2.1 (Meek 1980)
-0.6837Information measure for alpha-helix (Robson-Suzuki 1976)
-0.6879Retention coefficient at pH 2 (Guo et al. 1986)
-0.6977Retention coefficient at pH 2 (Guo et al. 1986)
-0.7037Optical rotation (Fasman 1976)
-0.7079Retention coefficient in TFA (Browne et al. 1982)
-0.7087Retention coefficient in TFA (Browne et al. 1982)
-0.7129Volumes including the crystallographic waters using the ProtOr (Tsai et al.
-0.7157The Kerr-constant increments (Khanarian-Moore 1980)
-0.7349Optical rotation (Fasman 1976)
-0.7399Average volumes of residues (Pontius et al. 1996)
-0.7397Refractivity (McMeekin et al. 1964) Cited by Jones (1975)
-0.7449Average side chain orientation angle (Meirovitch et al. 1980)
-0.7447Residue accessible surface area in folded protein (Chothia 1976)
-0.7489The Kerr-constant increments (Khanarian-Moore 1980)
-0.7517Average side chain orientation angle (Meirovitch et al. 1980)
-0.7609Residue accessible surface area in folded protein (Chothia 1976)
-0.7709Refractivity (McMeekin et al. 1964) Cited by Jones (1975)
-0.7697Optimized average non-bonded energy per atom (Oobatake et al. 1985)
-0.7797Average accessible surface area (Janin et al. 1978)
-0.7867Average volumes of residues (Pontius et al. 1996)
-0.7959Optimized average non-bonded energy per atom (Oobatake et al. 1985)
-0.7987Residue volume (Goldsack-Chalifoux 1973)
-0.7999Average accessible surface area (Janin et al. 1978)