Isothermal Titration Calorimetry in Enzymology

Name: Isothermal Titration Calorimetry in Enzymology
Price: 175 USD
Availability: InStock
ISBN: 9780443218484

Techniques and Applications

by Anthony Mittermaier, Justin Di Trani

1st Edition

Publisher: Academic Press

(0 reviews)

Compare Prices

VitalSourceLifetime Access$175.00 Best PriceAmazonKindle$166.25 AlibrisLifetime Access$175.00

Book Details

Print ISBN	9780443218484
eText ISBN	9780443218491
Publisher	Academic Press
Publishing Year	2025
Edition	1st Edition
Language	English
Pages	354

Isothermal Titration Calorimetry in Enzymology, 1st Edition, offers practical methodology for using isothermal titration calorimetry to measure enzyme catalysis and active site interactions. The volume details binding events involving substrates, cofactors, inhibitors, and reaction products. Designed for biochemists, enzymologists, and cell biologists, this reference work establishes experimental frameworks for studying key kinetic and thermodynamic properties across diverse biological systems.

The thematic structure connects foundational thermodynamic principles with advanced kinetic analyses. Coverage integrates kinetics-based and thermodynamics-based calorimetry approaches, systematically moving from standard protocols for measuring binding rates to specialized analytical settings. These settings include in vivo enzyme kinetics and the characterization of catalytic behaviors inside crowded solution environments.

Practical case studies connect physical measurement theories to concrete biological problems, including aminoglycoside resistance enzymes and direct enzyme interactions with toxic metals. This coverage provides biotechnologists, biochemical engineers, chemists, chemical engineers, and students with targeted methodology for experimental design and quantitative data interpretation across academic and industrial laboratories.

Chapter 1: Enzyme kinetics by ITC
Chapter 2: Measuring binding kinetics by ITC
Chapter 3: Analysing ITC kinetic data with AFFinimeter software
Chapter 4: In vivo enzyme kinetics by ITC
Chapter 5: Characterizing enzyme kinetics by 2D-ITC
Chapter 6: Measuring enzyme stability using ITC
Chapter 7: Kinetics of immobilized enzymes
Chapter 8: Enzyme kinetics in crowded solutions
Chapter 9: Kinetics of nanozymes
Chapter 10: Using ITC to characterize enzyme allostery
Chapter 11: Signal amplification in ITC kinetics experiments
Chapter 12: ITC kinetic studies of 6-phytase
Chapter 13: Catalysis of biological substrates of nuclear metallohydrolases
Chapter 14: Alpha-amylase activity and inhibition
Chapter 15: Enzyme stability and activity of psycrophillic enzymes
Chapter 16: Non-MM kinetics of peroxidases and application to industrial wastes
Chapter 17: Kinetics of diphosphohydrolases
Chapter 18: Interpretation of ITC binding curves
Chapter 19: Analysis of ITC binding data using SEDPHAT
Chapter 20: ITC in drug discovery
Chapter 21: ITC in the development of cancer therapeutics
Chapter 22: Mechanisms of aminoglycoside resistance enzymes
Chapter 23: Using ITC to characterize the interactions of natural products with biomolecules
Chapter 24: ITC studies of metalloenzymes
Chapter 25: Enzyme interactions with toxic metals
Chapter 26: Thermodynamics of molecular machines
Chapter 27: Thermodynamics of protein chaperones
Chapter 28: Characterizing protein interactions in apoptosis by ITC
Chapter 29: Using ITC to study ubiquitination
Chapter 30: Thermodynamics of transition state analogs
Chapter 31: Thermodynamics of recombinant enzymes in biotechnology
Chapter 32: Ion Binding to Transport Proteins using ITC
Chapter 33: Urease from Helicobacter pylori, lessons from ITC
Chapter 34: Substrate recognition by Chitinases
Chapter 35: ITC studies of glycoside hydrolases