From: Computational re-engineering of Amylin sequence with reduced amyloidogenic potential
Original | Residue no. | Mutated | Disruption | TANGO |
---|---|---|---|---|
amino acid | amino acid | method | rank | |
A | 13 | R | Making core charged | 1 |
F | 15 | P | Mutating an amino acid on a beta strand | 2 |
F | 15 | D | Making core charged | 3 |
L | 16 | D | Making core charged | 4 |
A | 25 | R | Making core charged | 5 |
I | 26 | R | Making core charged | 6 |
G | 24 | P | Mutating GLY at a turn | 7 |
L | 27 | R | Making an amino acid on a beta strand charged | 8 |
F | 23 | E | Making core charged | 9 |
G | 24 | D | Making core charged | 10 |
V | 17 | E | Making core charged | 11 |
Q | 10 | H | Making protein surface hydrophobic | 12 |
N | 21 | P | Mutating an amino acid at a turn | 14 |
C | 2 | Q | Making protein surface hydrophobic | 15 |
T | 6 | M | Making protein surface hydrophobic | 16 |
T | 4 | S | Making protein surface hydrophobic | 17 |
V | 32 | K | Making an amino acid on a beta strand charged | 18 |
N | 3 | H | Making protein surface hydrophobic | 19 |
A | 8 | E | Making an amino acid on a beta strand charged | 20 |
T | 9 | N | Making protein surface hydrophobic | 21 |
L | 12 | E | making core charged | 23 |
C | 7 | T | Making protein surface hydrophobic | 24 |
G | 33 | E | Making an amino acid on a beta strand charged | 25 |
S | 20 | G | Discovered experimentally [29] | 13 |
S | 20 | K | Discovered experimentally [29] | 22 |
N | 21 | L | Discovered experimentally [56] | 26 |
N | 14 | L | Discovered experimentally [56] | 27 |