Fusion of barnase to antiferritin antibody F11 VH domain results in a partially folded functionally active protein

Biochemistry (Moscow)

Volumn 74, Issue 6, 2009, Pages 672-680

  Shubenok, D V ^a   Tsybovsky, Y I ^b   Stremovskiy, O A ^c   Deyev, S M ^c   Martsev, S P ^a  

^a Ministry of Health Republic of Belarus   (Belarus)

^b MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

^c SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Barnase; Differential scanning calorimetry; Immunofusion; Molten globule; Protein folding; VH domain

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE SPECTROSCOPY; MONOCLONAL ANTIBODIES; PROTEIN FOLDING; RECOMBINANT PROTEINS;

BACILLUS AMYLOLIQUEFACIENS; BARNASE; CD AND FLUORESCENCE SPECTROSCOPY; IMMUNOFUSION; INSOLUBLE AGGREGATES; MOLTEN GLOBULE; SECONDARY STRUCTURES; VH DOMAIN;

ADDITIVES;

BACILLUS AMYLOLIQUEFACIENS; BACTERIA (MICROORGANISMS);

ANTIBODY; ARGININE; BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; CHAPERONIN; FERRITIN; HYBRID PROTEIN; MONOCLONAL ANTIBODY; RIBONUCLEASE; RNA; SCF11 ANTIBODY; THIOL REAGENT;

ARTICLE; BACILLUS; BACTERIUM TRANSFORMATION; BIOSYNTHESIS; CHEMISTRY; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; GENETICS; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; SPECTROFLUOROMETRY;

ANTIBODIES; ANTIBODIES, MONOCLONAL; ARGININE; BACILLUS; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; ESCHERICHIA COLI; FERRITINS; GROEL PROTEIN; GROES PROTEIN; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RIBONUCLEASES; RNA; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL REAGENTS; TRANSFORMATION, BACTERIAL;

EID: 67650081362     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297909060121     Document Type: Article

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