Table 1.
Classification of BSLA substitutions at six positions that form additional salt bridges in OSs.
|
OS resistance |
Classification of amino acid substitution % (variants)[a] |
|||
|---|---|---|---|---|
|
|
Charged |
Polar |
Aromatic |
Aliphatic |
|
Beneficial |
7–17 % (2–5) |
0–2 % (0–1) |
6–11 % (1–2) |
0–7 % (0–2) |
|
|
|
|
|
|
|
Unchanged |
77–87 % (23–26) |
71–81 % (30–34) |
72–78 % (13–16) |
73–93 % (22–26) |
|
|
|
|
|
|
|
Decreased |
3–6 % (1–2) |
7–17 % (3–7) |
6–22 % (1–4) |
3–23 % (1–7) |
|
|
|
|
|
|
|
Inactive |
0 % |
12 % (5) |
6 % (1) |
3 % (1) |
[a] The amino acid positions 34, 35, 61, 64, 112, 144 were selected for statistical analysis. OSs include 22 % (v/v) DOX, 60 % (v/v) DMSO, and 12 % (v/v) TFE. Charged substitutions were the best choice for improving the OS resistance comparing to polar, aromatic, and aliphatic. The results of all individual amino acid exchanges are depicted in Figure 2 b.