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https://doi.org/10.1142/S0219030316000562Cited by:0 (Source: Crossref)
Abstract
High-Throughput Sequencing on a Next Generation Sequencer to Identify Specific Binders from a Phage Library
Antibody Solution Viscosity and Intermolecular Interactions: Considerations for Development of Highly Concentrated Formulations
Display of Membrane Proteins on a Viral Envelope for Antibody Generation
Sequence and Structural Determinants of Antigen Binding in Antibody CDR Loops
Enhancement of the Stability of Single Chain Fv Molecules with the Amino Acid Substitutions Predicted by High-Performance Computer
Thermal Stability of Camelid Single Domain VHH Antibody
Keywords:
- Antibody stability
- Chemical modification
- Denaturation
- Protein folding
- Protein thermal stability
- VHH antibody
- Membrane protein
- monoclonal antibody
- baculovirus
- immunotherapy
- cancer
- drug delivery system
- single chain Fv
- protein stability
- amino acid mutation
- computational prediction
- isothermal titration calorimetry
- protein engineering
- Antibody
- phage library
- next generation sequencer
- peptide
- selection
- biopanning
- antigen recognition
- antigen-binding tendency
- diversity of CDR-H3
- long CDR-H3 loops
- loop lengths
- hydrogen bond networks
- High viscosity
- concentrated antibody formulation
- analytical ultracentrifugation
- secondary virial coefficient
- electrostatic interactions
- dynamic light scattering
- camelid
