Understanding unfolding and refolding of the antibody fragment (Fab) III: Mapping covalent and non-covalent interactions during in-vitro refolding of light chain, heavy chain, and Fab.
- 1 November 2022
- journal article
- research article
- Published by Elsevier BV in Biochemical Engineering Journal
Abstract
No abstract availableFunding Information
- Department of Science and Technology, Ministry of Science and Technology, India (ECR/2017/000493)
- Council of Scientific and Industrial Research, India (MLP031126)
- University Grants Commission
- BIRAC (BT/NBM0161/04/19)
- Department of Biotechnology, Ministry of Science and Technology, India (BT/PR26640/NNT/28/1358/2017)
This publication has 62 references indexed in Scilit:
- Biophysical Characterization of Met-G-CSF: Effects of Different Site-Specific Mono-Pegylations on Protein Stability and AggregationPLOS ONE, 2012
- Aggregates in monoclonal antibody manufacturing processesBiotechnology & Bioengineering, 2011
- Identification of the Unpaired Cysteine Status and Complete Mapping of the 17 Disulfides of Recombinant Tissue Plasminogen Activator Using LC−MS with Electron Transfer Dissociation/Collision Induced DissociationAnalytical Chemistry, 2010
- Extrinsic Fluorescent Dyes as Tools for Protein CharacterizationPharmaceutical Research, 2008
- Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domainsProceedings of the National Academy of Sciences of the United States of America, 2006
- Domain Interactions in the Fab Fragment: A Comparative Evaluation of the Single-chain Fv and Fab Format Engineered with Variable Domains of Different StabilityJournal of Molecular Biology, 2005
- Mass spectrometry-based proteomicsNature, 2003
- Association of Antibody Chains at Different Stages of Folding: Prolyl Isomerization Occurs after Formation of Quaternary StructureJournal of Molecular Biology, 1995
- Molecular basis of co-operativity in protein foldingJournal of Molecular Biology, 1991
- Domain association in immunoglobulin molecules: The packing of variable domainsJournal of Molecular Biology, 1985