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Effect of Rotation on the Diffusion-Controlled Rate of Ligand-Protein Association
Terrell L. Hill
Proceedings of the National Academy of Sciences of the United States of America
Vol. 72, No. 12 (Dec., 1975), pp. 4918-4922
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/65316
Page Count: 5
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The rate of binding a fairly large ligand molecule to a protein is reduced below the usual diffusion-controlled rate by the requirement of a certain rotational orientation. A simple, approximate treatment of this effect is given for special cases of spherical and ellipsoidal ligands. As the center of an ellipsoidal ligand approaches a protein surface, there is an effective repulsive potential between ligand and surface owing to restricted rotation of the ligand. The frequency factor kT/h of the Eyring rate theory is replaced in these reactions involving diffusion in solution by D/RΛ , where D = diffusion coefficient of ligand, Λ = thermal deBroglie wavelength of ligand, and R = ``capture'' distance around the binding site on the protein.
Proceedings of the National Academy of Sciences of the United States of America © 1975 National Academy of Sciences