Table II.

Calculated characteristics for phages with mutations in 12–19 amino acids of pVIII protein

Structure of 12–19 amino acids	Phage concentrationa, vir ml−1	Kd, nM	N	lg Kd	S+, Å2	ET, kcal mol−1	rc, Å	HOMO, eV
DSLQASAT	3.2 × 1010	30.0	94	−7.52	171.887	17.393	6.282	−4.669
DSLHGQAM	1.6 × 1010	15.0	173	−7.82	162.731	11.586	6.504	−7.122
DQLNATAL	1.9 × 1010	17.8	255	−7.75	180.435	25.520	6.321	−6.297
AELTTRAE	2.5 × 1010	23.4	3404	−7.63	180.415	23.990	6.472	−3.777
DSLTLQAQ	4.0 × 1010	37.5	113	−7.43	176.641	21.736	6.769	−3.414
ADLTVQAN	5.0 × 1010	46.9	240	−7.33	174.261	16.383	6.772	−3.256
SNLEMMAT	6.0 × 1010	56.3	1043	−7.25	176.313	16.230	6.710	−2.804
DQLTVSAQ	6.0 × 1010	56.3	71	−7.25	187.865	22.031	6.938	−3.636
DTLTHEAT	8.0 × 1010	75.0	30	−7.12	185.024	17.715	6.510	−4.684
EDLTQRAL	27.0 × 1010	253.1	376	−6.60	201.178	18.395	6.985	−3.640

K_d, constant of dissociation. N, number of conformers. S₊, area of the positively charged surface. E_T, energy of torsion stresses. r_c, radius of the described cylinder. HOMO, energy of the upper occupied molecular orbital. ^aPhage concentration (vir ml⁻¹) estimated at the point of 50% binding of β-Gal in competition ELISA. The phage concentrations were determined by spectrophotometric measurement (for details, see Materials and methods).