The reduced form of the antibody CH2 domain

Among the immunoglobulin domains, the CH2 domain has the lowest thermal stability, which also depends on amino acid sequence and buffer conditions. To further identify factors that influence CH2 folding and stability, we characterized the domain in the reduced form using differential scanning fluori...

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Bibliographic Details
Published in:	Protein science 2021-09, Vol.30 (9), p.1895-1903
Main Authors:	Xi, Zhaoyong, Liu, Xianglei, Lin, Rui, Persons, John D., Ilina, Tatiana V., Li, Wei, Dimitrov, Dimiter S., Ishima, Rieko
Format:	Article
Language:	English
Subjects:	Amino Acid Sequence Amino acids Antibodies antibody CH2 Cloning, Molecular Disulfides - chemistry Disulfides - metabolism disulfide‐bridge Domains Escherichia coli - genetics Escherichia coli - metabolism Fluorimetry Full‐Length Paper Full‐Length Papers Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Humans Immunoglobulin Domains - genetics Immunoglobulin G - chemistry Immunoglobulin G - genetics Immunoglobulin G - metabolism Models, Molecular NMR Nuclear magnetic resonance Oxidation-Reduction Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Denaturation Protein Engineering Protein Interaction Domains and Motifs Protein Stability Protein Structure, Tertiary Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism thermal denaturation Thermal stability Thermodynamics
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