Feig, Andrew L's Calorimetry PDF

By Feig, Andrew L

ISBN-10: 0128029064

ISBN-13: 9780128029060

ISBN-10: 0128029072

ISBN-13: 9780128029077

Calorimetry, the most recent quantity within the Methods in Enzymology sequence maintains the legacy of this most desirable serial with caliber chapters authored through leaders within the box. Calorimetry is a hugely technical test and it's easy for brand new practioners to get fooled into studying artifacts as actual experimental results.  This quantity will consultant readers to get the main out in their beneficial organic samples and contains themes on particular protocols for the categories of reviews being performed in addition to how one can enhance the knowledge assortment. most significantly, the chapters also will aid to spot pitfalls that must be shunned to make sure that the best quality effects are obtained.

  • Contains well timed contributions from well-known specialists during this  speedily altering field
  • Provides particular protocols and the right way to increase info assortment and make sure the very best quality effects are acquired Covers study tools in calorimetry, and contains sections on subject matters reminiscent of differential scanning calorimetry of membrane and soluble proteins in detergents.

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Third, 52 Michael I. Recht et al. fragment to lead with a low molecular weight starting point (average MW % 150 Da), provides sufficient room to grow the molecule while staying within successfully launched drug chemical space (MW < % 350–400 Da) (Wenlock, Austin, Barton, Davis, & Leeson, 2003). , selectivity) can provide multiple chemically diverse starting points for lead optimization. The ability of calorimetry to provide accurate KI for low molecular weight, weakly binding ligands during the screening and lead optimization phases allows for more accurate structure-activity relationship development early in the fragment-to-lead stage of the discovery process.

2004). Each detector cell on the array consists of two identical thermistor sensing elements connected in a Wheatstone bridge configuration that provides a differential temperature measurement between the sample specimen and reference specimen (Fig. , 2004). , 2004) À6 Throughput [Enzyme] (Per hour) (M) 1 Â 10À10 5 Â 10À8 kcat is the turnover number, KM is the Michaelis constant, and KI is the competitive inhibition constant. Enzyme concentration and moles of enzyme and substrate are calculated assuming kcat ¼ 2 sÀ1, KM ¼ 5 μM, [S]0 (enthalpy array) ¼ 300 Â KM, [S]0 (ITC) ¼ 50 Â KM, ΔH ¼ À5000 cal/mol, and throughput as indicated in table.

Although we have only shown a single titration at each temperature for clarity in the figures presented here (Fig. 5), we generally find fitting of triplicate titrations at each selected temperature to provide a more robust sampling of the errors associated with the measurements. For the case study we present, our experiments demonstrate that the FCP1–Rap74 interaction is readily reversed and characterized by a modest equilibrium dissociation constant of 2–5 μM under nearly all assayed conditions.

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Calorimetry by Feig, Andrew L

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