Author: Justina Jankauskaite; Brian Jiménez-García; Justas Dapkunas; Juan Fernández-Recio; Iain H. Moal
Title: SKEMPI 2.0: An updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutation Document date: 2018_6_7
ID: d0eynz67_24_1
Snippet: in which the removal of the F136 side-chain of MlC creates a large cavity at the binding interface, the addition of a phenylalanine at the A451 position of IIB Glc creates a large clash, however the double mutation creates an interaction that is even more stable than the wild-type by creating an anchor residue across the binding interface in which the cavity in MlC is filled by the new side-chain of IIB......
Document: in which the removal of the F136 side-chain of MlC creates a large cavity at the binding interface, the addition of a phenylalanine at the A451 position of IIB Glc creates a large clash, however the double mutation creates an interaction that is even more stable than the wild-type by creating an anchor residue across the binding interface in which the cavity in MlC is filled by the new side-chain of IIB.
Search related documents:
Co phrase search for related documents- anchor residue and wild type: 1, 2
- bind interface and wild type: 1, 2
- binding interface and large cavity: 1, 2
- binding interface and wild type: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18
- double mutation and wild type: 1, 2, 3, 4, 5, 6
- large cavity and wild type: 1
Co phrase search for related documents, hyperlinks ordered by date