Variations in Antigen−Antibody Association Kinetics as a Function of pH and Salt Concentration: A QSAR and Molecular Modeling Study-Reference-Cited by-同舟云学术

Variations in Antigen−Antibody Association Kinetics as a Function of pH and Salt Concentration: A QSAR and Molecular Modeling Study

Published:2005-10-12 Issue:44 Volume:44 Page:14409-14418
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dejaegere Annick¹,Choulier Laurence¹,Lafont Virginie¹,De Genst Erwin¹,Altschuh Danièle¹

Affiliation:

1. UMR 7175-LC1, CNRS/ULP, ESBS, Parc d'Innovation, Bld S. Brant, BP 10413, 67412 Illkirch Cedex, France, UMR 7104, Structural Biology and Genomics Department, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 10142 F-67404 Illkirch Cedex, France, and Laboratory of Cellular and Molecular Immunology, Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut vor Biotechnologie, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi050986v

Reference46 articles.

1. Degenerate interfaces in antigen-antibody complexes

2. Antigen Specificity and High Affinity Binding Provided by One Single Loop of a Camel Single-domain Antibody

3. Analysis of the pH-dependencies of the association and dissociation kinetics of HIV-1 protease inhibitors

4. Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFNα2 1 1Edited by A. R. Fersht

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