In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state

Protein Science

Volumn 5, Issue 10, 1996, Pages 2089-2094

  Subramaniam, Vinod ^a,b,d   Steel, Duncan G ^a,b   Gafni, Ari ^b,c  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^d MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

bovine lactoglobulin; protein folding; protein lability; protein structure; spectroscopy; tryptophan phosphorescence

Indexed keywords

ANIMAL CELL; ANTIBODY SPECIFICITY; ARTICLE; CHEMICAL REACTION; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

ANIMALIA; BOVINAE; ESCHERICHIA COLI;

EID: 0029911537     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051015     Document Type: Article

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