Table 1.

Summary of computations at 25°C

Peptide sequence	No. of generated conformations*	No. of accepted conformations	Lowest energy, Kcal/mol	Helical fraction θcoupling, %	Helical fraction θdihedral, %	Dielectric constant ɛ
ALA16	43,752	1,345	−255.8	7 (6†)	12 (6†)	80
ALA16	42,256	1,222	−215.7	59	68	40
ALA16	49,151	1,416	−79.8	90	100	2
ALA10	50,824	1,645	−181.6	0 (0‡)	10 (0‡)	80
ALA10	34,105	1,626	−154.0	54	71	40
ALA10	45,357	1,739	−49.5	90	100	2
9A1K§	38,482	1,649	−176.5	77	76	80
9A1Q	39,381	1,689	−252.5	31	50	80

^*These values correspond to the number of generated conformations for the runs using the procedure described in refs 11 and 12. 

^† Theoretical estimates obtained by using the experimental value of the Zimm-Bragg parameters (2), as derived from Host-Guest experiments (3), i.e., σ = 8 × 10⁻⁴ and s = 1.06 at 25°C. 

^‡ Experimental value obtained by using the tri-block copolymer technique for the thermally induced helix-coil transition for copolymers of the type (d,l-lysine)_m-(l-alanine)_n-(d,l-lysine)_m, with n = 10 for the alanyl residues in the central block (1). 

^§ Values in this row were computed at pH 6, with a value of 10.5 adopted for pK_a⁰ for the lysine residue (14).