Empty and Peptide-Loaded Class II Major Histocompatibility Complex Proteins Produced by Expression inEscherichia coliand Foldingin Vitro
The human class II major histocompatibility complex protein HLA–DR1 has been expressed
inEscherichia colias denatured α and β subunits and foldedin vitroto form the native
structure. DR1 folding yields are 30–50% in the presence or absence of tight-binding
antigenic peptides. The protein produced in this manner is soluble and monomeric with the
expected apparent molecular weight. It reacts with conformation-sensitive anti-DR
antibodies and exhibits peptide-dependent resistance to SDS-induced chain dissociation …
inEscherichia colias denatured α and β subunits and foldedin vitroto form the native
structure. DR1 folding yields are 30–50% in the presence or absence of tight-binding
antigenic peptides. The protein produced in this manner is soluble and monomeric with the
expected apparent molecular weight. It reacts with conformation-sensitive anti-DR
antibodies and exhibits peptide-dependent resistance to SDS-induced chain dissociation …