Table IV.

Contributions Made by the Hydrophobic and Hydrophilic Non-hydrogen Atoms to the SASA (nm²) and the rgyr (nm) of the Different α- and β-peptide Systems Described in Table II During 10 ns of MD Simulation with the 53A6 GROMOS Force Field⁷

	SASA(Whole Peptide)			SASA(Per Atoma)
Peptide	Hydrophobic	Hydrophilic	Total	Hydrophobic	Hydrophilic	Total	rgyr
αMO—	9.42	3.72	13.14	0.39	0.22	0.32	0.40
αMOH	9.78	3.15	12.93	0.41	0.19	0.32	0.40
αWO—	6.70	2.20	8.89	0.28	0.13	0.22	0.40
αWOH	6.87	1.88	8.75	0.29	0.11	0.21	0.40
βMO—	10.03	2.03	12.06	0.42	0.16	0.33	0.35
βMOH	10.26	1.91	12.18	0.43	0.15	0.33	0.35
βWO—	6.59	1.47	8.06	0.27	0.11	0.22	0.35
βWOH	6.81	1.29	8.10	0.28	0.10	0.22	0.35

^aThe α- and β-peptides both have 24 hydrophobic atoms. The α-peptide has 17 hydrophilic atoms and the β-peptide 13.