Helix initiation parameter at posision i-1 (Finkelstein et al., 1991)

Finkelstein, A.V., Badretdinov, A.Y. and Ptitsyn, O.B.

Physical reasons for secondary structure stability: alpha-helices in short peptides

Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1.7 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 0.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 )

Helix initiation parameter at posision i,i+1,i+2 (Finkelstein et al., 1991)

Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 0.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 ) (Pro !)

Helix termination parameter at posision j-2,j-1,j (Finkelstein et al., 1991)

Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 1.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 )

Helix termination parameter at posision j+1 (Finkelstein et al., 1991)

Partition coefficient (Garel et al., 1973)

Coefficients de partage d'aminoacides, nucleobases, nucleosides et nucleotides dans un systeme solvant salin

Amino acid preferences for secondary structure vary with protein class

Alpha-helix indices for alpha-proteins (Geisow-Roberts, 1980)

Alpha-helix indices for beta-proteins (Geisow-Roberts, 1980)

Alpha-helix indices for alpha/beta-proteins (Geisow-Roberts, 1980)

Beta-strand indices for beta-proteins (Geisow-Roberts, 1980)

Beta-strand indices for alpha/beta-proteins (Geisow-Roberts, 1980)

Aperiodic indices for alpha-proteins (Geisow-Roberts, 1980)

Aperiodic indices for beta-proteins (Geisow-Roberts, 1980)

Aperiodic indices for alpha/beta-proteins (Geisow-Roberts, 1980)

Contribution of the free energy of mixing of hydrophobic side chains to the stability of the tertiary structure