Chimeras of human lysozyme and α-lactalbumin: An interesting tool for studying partially folded states during protein folding

Cellular and Molecular Life Sciences

Volumn 54, Issue 11, 1998, Pages 1217-1230

  Van Dael, H ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

lactalbumin; Chimera; Folding intermediates; Lysozyme; Molten globule; Protein engineering; Protein folding; Stability

Indexed keywords

ALPHA LACTALBUMIN; CHIMERIC PROTEIN; LYSOZYME;

CHIMERA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MODIFICATION; REVIEW;

AMINO ACID SEQUENCE; HUMANS; LACTALBUMIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; TEMPERATURE;

EID: 0031794305     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050249     Document Type: Review

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