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. 2009 Jan 22;52(2):225-33.
doi: 10.1021/jm800498e.

Beyond picomolar affinities: quantitative aspects of noncovalent and covalent binding of drugs to proteins

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Beyond picomolar affinities: quantitative aspects of noncovalent and covalent binding of drugs to proteins

Adam J T Smith et al. J Med Chem. .
No abstract available

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Figures

Figure 1
Figure 1
Summary of the typical binding constants for host–guest complexes. For each class, the binding distribution is represented by an idealized normal distribution. Each curve is normalized to have the same area, the maximum occurs at the average value of Ka, and the standard deviation is used to set the width of the curve. Reprinted with permission from reference . Copyright 2005 Americal Chemical Society.
Figure 2
Figure 2
Plot of log Ka versus buried solvent accessible surface area (ΔSASA). Reprinted with permission from reference . Copyright 2005 Americal Chemical Society.
Figure 3
Figure 3
Frequency plot of association constant for 507 antibody–antigen complexes, 160 enzyme–inhibitor complexes, and 1017 measurements of enzyme–transition state complex. Reprinted with permission from reference . Copyright 2005 Americal Chemical Society.

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