| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2029928 | Structure | 2010 | 12 Pages |
Abstract
⺠apo IGPS displays few millisecond motions ⺠Allosteric ligand binding is entropically dominated ⺠Protein-wide millisecond motions are enhanced upon allosteric ligand binding ⺠The flexible residues form a continuous network between active sites
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Authors
James M. Lipchock, J. Patrick Loria,