Titlebook: Microcalorimetry of Biological Molecules; Methods and Protocol Eric Ennifar Book 2019 Springer Science+Business Media, LLC, part of Springe

MOTTO

Characterization of Microtubule-Associated Proteins (MAPs) and Tubulin Interactions by Isothermal Tiodynamic method that enables a full thermodynamic characterization of the interaction after a single titration experiment. We provide here the protocols to apply ITC to tubulin interaction with either stathmin or tau, which will help to avoid the common pitfalls in this very powerful and sensitive method.

BILIO

Climate

實(shí)施生效

High-Quality Data of Protein/Peptide Interaction by Isothermal Titration Calorimetryr the protein, making the sample quality and data acquisition all the more critical. This chapter emphasizes more specifically the relevance of those points to improve the reproducibility of ITC measurements and to gain high-quality thermodynamic parameters.

Arctic

合唱隊(duì)

Tinkering with Binding Polynomials in Isothermal Titration Calorimetryr handling the complexities that can be encountered when studying macromolecule-ligand interactions, though it has been deemed troublesome. The goal of this chapter is to provide a quite simple and widely available set of training experiments aimed at mastering the formalism of the binding polynomial applied to isothermal titration calorimetry.

新奇

諷刺滑稽戲劇

Isothermal Titration Calorimetry Measurements of Riboswitch-Ligand Interactionsl or translational output. For over a decade, isothermal titration calorimetry (ITC) has been used to investigate how riboswitches interact with small molecules. We present methods for assaying RNA-ligand interactions using ITC and analyzing resulting data to estimate thermodynamic parameters associated with binding.

adumbrate

GRIPE