Allostery : methods and protocols /

Other Authors: Fenton, Aron W.
Format: Book
Language: English
Published: New York : Humana Press : 2011
Series: Methods in molecular biology (Clifton, N.J.) ; v. 796.
Springer protocols (Series)
Online Access: Get full text
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Table of Contents:
  • Binding techniques to study the allosteric energy cycle
  • Kinetic trapping of a key hemoglobin intermediate
  • Allosteric coupling between transition metal-binding sites in homooligomeric metal sensor proteins
  • Studying the allosteric energy cycle by isothermal titration calorimetry
  • Detecting "Silent" Allosteric coupling
  • Using mutant cycle analysis to elucidate long-range functional coupling in allosteric receptors
  • A review of methods used for identifying structural changes in a large protein complex
  • Allosteric mechanisms of g protein-coupled receptor signaling: A structural perspective
  • Dynamic light scattering to study allosteric regulation
  • Dissecting the linkage between transcription factor self-assembly and site-specific DNA binding: The role of the analytical ultracentrifuge
  • Fluorescence correlation spectroscopy and allostery: The case of GroEL
  • The morpheein model of allostery: Evaluating proteins as potential morpheeins
  • Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions
  • Hydrogen-deuterium exchange study of an allosteric energy cycle
  • Ensemble properties of network rigidity reveal allosteric mechanisms
  • An in vivo approach to isolating allosteric pathways using hybrid multimeric proteins
  • Mutations in the GABA(A) receptor that mimic the allosteric ligand etomidate
  • Allosteric regulation of human liver pyruvate kinase by peptides that mimic the phosphorylated/dephosphorylated N-terminus
  • In silico-screening approaches for lead generation: Identification of novel allosteric modulators of human-erythrocyte pyruvate kinase
  • Identification of allosteric-activating drug leads for human liver pyruvate kinase
  • A critical evaluation of correlated mutation algorithms and coevolution within allosteric mechanisms
  • The advantage of global fitting of data involving complex linked reactions
  • Predicting binding sites by analyzing allosteric effects.