In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway, folding initiation site, and potential role of C-peptide in folding process

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 17800-17809

  Qiao, Zhi Song ^a   Min, Cheng Yin ^a   Hua, Qing Xin ^b   Weiss, Michael A ^b   Feng, You Min ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CHEMICAL BONDS; CONFORMATIONS; MOLECULAR STRUCTURE; QUENCHING;

DOUBLE-CHAIN PEPTIDE;

INSULIN;

C PEPTIDE; PROINSULIN; AMINO ACID; CYSTEINE; DISULFIDE; LYSINE; OXYGEN; PEPTIDE; PROTEINASE; RECOMBINANT PROTEIN;

ALPHA HELIX; ARTICLE; BETA CHAIN; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DISULFIDE BOND; HUMAN; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMISTRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; PEPTIDE MAPPING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SWINE; TIME;

SUIDAE;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BINDING SITES; C-PEPTIDE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; CYSTEINE; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASES; HUMANS; KINETICS; LYSINE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OXYGEN; PEPTIDE MAPPING; PEPTIDES; PROINSULIN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SWINE; TIME FACTORS;

EID: 0038043253     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M300906200     Document Type: Article

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