Direct Determination of Vibrational Density of States Change on Ligand Binding to a Protein
Author(s) -
Erika Balog,
Torsten Becker,
Martin Oettl,
R.E. Lechner,
Roy M. Daniel,
John Finney,
Jeremy C. Smith
Publication year - 2004
Publication title -
physical review letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.688
H-Index - 673
eISSN - 1079-7114
pISSN - 0031-9007
DOI - 10.1103/physrevlett.93.028103
Subject(s) - binding energy , dihydrofolate reductase , ligand (biochemistry) , inelastic scattering , materials science , atomic physics , physics , scattering , chemistry , nuclear magnetic resonance , enzyme , receptor , quantum mechanics , biochemistry
The change in the vibrational density of states of a protein (dihydrofolate reductase) on binding a ligand (methotrexate) is determined using inelastic neutron scattering. The vibrations of the complex soften significantly relative to the unbound protein. The resulting free-energy change, which is directly determined by the density of states change, is found to contribute significantly to the binding equilibrium
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