Low-Affinity Binding Determined by Titration Calorimetry Using a High-Affinity Coupling Ligand: A Thermodynamic Study of Ligand Binding to Protein Tyrosine Phosphatase 1B-Reference-Cited by-同舟云学术

Low-Affinity Binding Determined by Titration Calorimetry Using a High-Affinity Coupling Ligand: A Thermodynamic Study of Ligand Binding to Protein Tyrosine Phosphatase 1B

Published:1998-08 Issue:2 Volume:261 Page:139-148
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Zhang Yan-Ling,Zhang Zhong-Yin

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference32 articles.

1. Rapid measurement of binding constants and heats of binding using a new titration calorimeter

2. Isothermal Titration Microcalorimetric Studies for the Binding of Octenoyl-CoA to Medium Chain Acyl-CoA Dehydrogenase

3. Structural energetics of peptide recognition: Angiotensin II/antibody binding

4. Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase 1 1Edited by P. E. Wright

5. Counting the calories to stay in the groove

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