Heterogeneity in Disulfide Bond Reduction in IgG1 Antibodies Is Governed by Solvent Accessibility of the Cysteines

We studied unpaired cysteine levels and disulfide bond susceptibility in four different <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>γ</mi></semantics></math></inline-formula>-immunoglobulin antibodies using liquid chromatography–mass spectrometry....

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Autori principali:	Ramakrishnan Natesan, Andrew B. Dykstra, Akash Banerjee, Neeraj J. Agrawal
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	MDPI AG 2023-12-01
Serie:	Antibodies
Soggetti:	peptide mapping differential alkylation disulfide bond molecular dynamics SASA
Accesso online:	https://www.mdpi.com/2073-4468/12/4/83
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