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Catalytic Turnover

Why study dynamics?. Catalytic Turnover. Signaling/Regulation. ?. Δ G, Δ S , Δ H. Protein folding pathways and intermediates. Thermodynamics – entropy and heat capacity. Kleckner & Foster, BBA - Proteins and Proteomics, 2010. Typical Protein Motions and Timescales. 10 3. 10 0.

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Catalytic Turnover

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  1. Why study dynamics? Catalytic Turnover Signaling/Regulation ? ΔG, ΔS, ΔH Protein folding pathways and intermediates Thermodynamics – entropy and heat capacity Kleckner & Foster, BBA - Proteins and Proteomics, 2010

  2. Typical Protein Motions and Timescales 103 100 10-3 10-6 10-9 10-12 ks s ms us ns ps Global unfolding Local unfolding NH librations/ vibrations Overall Tumbling Chemical kinetics Slow loop reorientation Fast loop reorientation Motions

  3. H H N N S2 low 1.0 S2 0.0 Residue S2 high Local Motions – Model-free Formalism Order parameter (S2) Describes the amplitude of NH bond motion or the spatial restriction of the NH bond. Ranges in value from 0 to 1.

  4. H H N N S2 low, τe long S2 te S2 high τe short Residue Local Motions – Model-free Formalism Internal correlation time (τe) Describes the characteristic time it takes the NH bond to explore the space available to it. Can range from 30-400 ps.

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