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Beni-Suef University Journal of Basic and Applied Sciences

Table 5 MutaBind2 mutation-induced change in binding affinity prediction

From: Computer-aided molecular modeling and structural analysis of the human centromere protein–HIKM complex

Chain(s)

Mutation(s)

ΔΔGBinding (Kcal/mol)

H

L219A

1.95

H

V225A

0.28

H

L233A

0.8

H

K234A

0.13

H

L238A

2.18

M

L94A

1.88

M

L163E

0.7

  1. The input requires the PDB structure of the protein complex with a minimum of two distinct chains
  2. A negative and positive ΔΔGbind (kcal/mol) value correspond to stabilizing and destabilizing mutations, predicted to increase and decrease the binding affinity, respectively
  3. An all-positive value for the MutaBind2 output denotes a destabilizing effect on the protein–protein interaction
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