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. Author manuscript; available in PMC: 2020 May 1.

Published in final edited form as: J Struct Biol. 2019 Mar 14;206(2):193–203. doi: 10.1016/j.jsb.2019.03.003

Table 2.

α-Helical contents of truncated PAM_AP53 peptides and naturally occurring PAMs

Protein	% α-helices			θ₂₂₂/θ₂₀₈
Protein	4° C	25° C^a	37° C	4° C	25° C	37° C
PAM_{AP53_short}	75	39	30	0.92	0.74	0.69
PAM_{AP53_medium}	84	32	25	1.00	0.73	0.70
PAM_AP53-long	84	49	28	1.08	0.96	0.86
PAM_AP53	33	27	20	1.03	0.95	0.92
PAM_NS88.2	43	33	21	1.04	0.94	0.89
PAM_NS223	75	61	40	1.02	0.95	0.87
PAM_NS455	96	72	42	1.05	0.95	0.82
PAM_SS1448	52	33	22	1.04	0.92	0.87
PAM_SS1572	79	59	44	1.03	0.95	0.91
PAM_SS1574	61	54	29	1.05	1.01	0.89

^a

The percentage of α-helix in each PAM at 25° C was published previously (Qiu et al., 2018) and relisted here for comparison purposes.