Abstract
Combination of elementary functions. Transition of substrate from one active site to another. “Double sieve” increases specificity of function. Relative independence of protein folds from their elementary catalytic functions. Different catalytic sites can perform the same job. Ser-proteases and metalloproteinases. Multicharged ions. Visible connection between protein fold and protein environment. Combination of elementary protein functions and flexibility of protein structure. Induced fit. Mobility of protein domains. Shuffling of domains and protein evolution. Domain structure: kinases, dehydrogenases. Co-factors. Allostery: interaction of active sites. Allosteric regulation of protein function. Allostery and protein quaternary structure. Hemoglobin and myoglobin. Mechanochemical cycle. Kinesin: a bipedal protein. Mechanism of muscle contraction. Rotary motors.
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