Changes in Calorimetric Parameters and Solvent Accessibility of Hydrophobic Groups in Native and Chemically Modified Immunoglobulin G-Reference-Cited by-同舟云学术

Changes in Calorimetric Parameters and Solvent Accessibility of Hydrophobic Groups in Native and Chemically Modified Immunoglobulin G

Published:2000-05-01 Issue:20 Volume:104 Page:4980-4985
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Relkin P.¹,Kamyshny A.²,Magdassi S.²

Affiliation:

1. Laboratoire de Biophysique des Materiaux Alimentaires, Département Science de l’Aliment, Ecole Nationale Supérieure des Industries Alimentaires, 1, Avenue des Olympiades, 91744 Massy, France

2. Casali Institute of Applied Chemistry, The Hebrew University of Jerusalem, 91904, Jerusalem, Israel

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp993350k

Reference27 articles.

1. The Three-Dimensional Structure at 6 A Resolution of a Human γG1 Immunoglobulin Molecule

2. Changes of the Conformation of Rabbit IgG Antibody Caused by the Specific Binding of a Hapten. X-Ray Small-Angle Studies

3. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-.ANG. resolution

4. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution

5. Hydrophobically modified human IgG: surface and biological activities

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