Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis

Protein Science

Volumn 11, Issue 12, 2002, Pages 2932-2946

  De Laureto, Patrizia Polverino ^a   Frare, Erica ^a   Gottardo, Rossella ^a   Van Dael, Herman ^b   Fontana, Angelo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Circular dichroism; Lactalbumin; Limited proteolysis; Lysozyme; Molten globule; Protein folding

Indexed keywords

LACTALBUMIN; LYSOZYME; PEPSIN A; PROTEINASE; PROTEINASE K;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME SPECIFICITY; GENE DISRUPTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SPECTROSCOPY; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; CHICKEN; COMPARATIVE STUDY; DOG; HORSE; METABOLISM; MOLECULAR GENETICS; PIGEONS AND DOVES; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

BOVINAE; CANIS FAMILIARIS; COLUMBA; EQUUS CABALLUS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHICKENS; CIRCULAR DICHROISM; COLUMBIDAE; DOGS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE K; ENDOPEPTIDASES; HORSES; LACTALBUMIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; PEPSIN A; PROTEIN FOLDING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

EID: 0036891687     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0205802     Document Type: Article

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