The usefulness of bovine serum albumin (BSA) as a model protein for testing NMR methods for the study of protein-ligand interactions is discussed. Isothermal titration calorimetry established the binding affinity and stoichiometry of the specific binding site for L-tryptophan, D-tryptophan, naproxen, ibuprofen, salicylic acid and warfarin. The binding affinities of the same ligands determined by NMR methods are universally weaker (larger KD). This is because the NMR methods are susceptible to interference from additional non-specific binding. The L-tryptophan-BSA and naproxen-BSA systems were the best behaved model systems.

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particle-finding Nobel laureate, remembered p.185 CONSERVATION Dams threaten one of the world's largest inland fisheries p.184 VISION Reflections of a researcher who threw peas at hoverflies p.182 PUBLIC HEALTH Lessons for next time from the front lines of an Ebola outbreak p.180 To solve real-world problems using emerging abilities in synthetic biology, research must focus on a few ambitious goals, argues Dan Fletcher. Children receiving blood transfusions in Bangladesh, where maintaining the supply from donors can be more challenging than in wealthy countries.