Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 20, Issue 5, Pages 598-605Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2010.09.001
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Funding
- National Institutes of Health (USA) [R01EB009191, R01GM077435]
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R01EB009191] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM077435] Funding Source: NIH RePORTER
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Higher throughput thermodynamic measurements can provide value in structure-based drug discovery during fragment screening, hit validation, and lead optimization Enthalpy can be used to detect and characterize ligand binding, and changes that affect the interaction of protein and ligand can sometimes be detected more readily from changes in the enthalpy of binding than from the corresponding free-energy changes or from protein-ligand structures Newer higher throughput calorimeters are being incorporated into the drug discovery process Improvements in titration calorimeters come from extensions of a mature technology and face limitations in scaling Conversely, array calorimetry, an emerging technology, shows promise for substantial improvements in throughput and material utilization but improved sensitivity is needed
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