Folding and stability of chimeric immunofusion VL-barstar

A chimeric protein VL-barstar that comprises the VL domain of anti-human ferritin monoclonal antibody F11 and barstar, the naturally occurring inhibitor of bacterial RNase barnase, has been constructed for study of structure-function characteristics of chimeric immunoglobulin fused proteins. Such ch...

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Veröffentlicht in:	Biochemistry (Moscow) 2004-09, Vol.69 (9), p.939-948
Hauptverfasser:	Tsybovsky, Y I, Shubenok, D V, Stremovskiy, O A, Deyev, S M, Martsev, S P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anilino Naphthalenesulfonates - chemistry Antibodies Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - physiology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - physiology Calorimetry Calorimetry, Differential Scanning Circular Dichroism E coli Enzyme-Linked Immunosorbent Assay Escherichia coli Escherichia coli - chemistry Ferritins - chemistry Ferritins - physiology Humans Hydrogen-Ion Concentration Molecular Sequence Data Protein Binding Protein Denaturation - physiology Protein Folding Protein Structure, Tertiary - physiology Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - physiology Ribonucleases - chemistry Ribonucleases - physiology Temperature Viral antibodies
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