Impact of deglycosylation and thermal stress on conformational stability of a full length murine igG2a monoclonal antibody: Observations from molecular dynamics simulations

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 3, 2013, Pages 443-460

  Wang, Xiaoling ^a   Kumar, Sandeep ^a   Buck, Patrick M ^a   Singh, Satish K ^a  

^a PFIZER INC   (United States)

Author keywords

Biotherapeutics; Molecular dynamics; Monoclonal antibody; Simulation; Structure

Indexed keywords

AMINO ACID; FC RECEPTOR; IMMUNOGLOBULIN G2A ANTIBODY; MONOCLONAL ANTIBODY; SOLVENT;

ANTIBODY STRUCTURE; ANTIGEN BINDING; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DEGLYCOSYLATION; HIGH TEMPERATURE; IMMUNOGLOBULIN AGGREGATE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DATABASE; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; SIMULATION; TEMPERATURE STRESS;

ANIMALS; ANTIBODIES, MONOCLONAL, MURINE-DERIVED; COMPLEMENTARITY DETERMINING REGIONS; GLYCOSYLATION; HOT TEMPERATURE; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; MICE; MOLECULAR DYNAMICS SIMULATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; SOLVENTS; STRESS, PHYSIOLOGICAL; TIME FACTORS;

MURINAE;

EID: 84873093812     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24202     Document Type: Article

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