TABLE 3.

Effects of MTSC22 resistance mutations on the α-helicity and thermostability of 6-HB structure^a

NHR mutation type and peptide complex	[θ]222	Helix content (%)	Tm (°C)
Primary
SC22+N36	−28,470	86	64
SC22+N36E49K	−31,360	95	61
SC22+N36L57R	−28,586	86	37
SC22+N36E49k/L57R	−20,052	61	32
MTSC22+N36	−31,170	94	77
MTSC22+N36E49K	−28,570	87	72
MTSC22+N36L57R	−28,150	85	40
MTSC22+N36E49k/L57R	−21,683	66	35
HP23+N36	−31,877	97	86
HP23+N36E49K	−30,246	92	83
HP23+N36L57R	−30,441	92	49
HP23+N36E49k/L57R	−28,102	85	45
C34+N36	−33,190	101	64
C34+N36E49K	−31,240	95	70
C34+N36L57R	−35,014	106	55
C34+N36E49k/L57R	−33,757	102	60
SFT+N36	−31,389	95	71
SFT+N36E49K	−30,292	92	77
SFT+N36L57R	−32,819	100	62
SFT+N36E49k/L57R	−34,625	105	69
Secondary
N36+C34N126K	−27,708	84	70
N36+C34E136G	−27,700	84	62
N36+C34N126K/E136G	−26,229	80	65
N36E49K+C34N126K	−34,893	105	74
N36E49K+C34E136G	−33,386	101	66
N36L57R+C34N126K	−33,557	102	57
N36L57R+C34E136G	−36,014	109	50
N36E49K+C34N126K/E136G	−34,900	106	67
N36L57R+C34N126K/E136G	−35,929	108	51
N36E49K/L57R+C34N126K	−33,086	100	62
N36E49K/L57R+C34E136G	−35,414	107	54
N36E49K/L57R+C34N126K/E136G	−32757	99	55

^aThe α-helicity and thermostability of 6-HBs were measured by CD spectroscopy, and the experiments were repeated at least twice to verify the results.