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Volumn 7, Issue 3, 2015, Pages 525-539

Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody

Author keywords

Aggregation; Flexibility; High protein concentration; Hydrogen exchange; Immunoglobulin G1; Mass spectrometry; Monoclonal antibody; Protein protein interactions; Reversible self association; Stability

Indexed keywords

DEUTERIUM; HYDROGEN; IMMUNOGLOBULIN G1; MONOCLONAL ANTIBODY; PEPTIDE; COMPLEMENTARITY DETERMINING REGION; IMMUNOGLOBULIN G;

EID: 84938844658     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2015.1029217     Document Type: Article
Times cited : (70)

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