Probing residue-level unfolding during lysozyme precipitation

Biotechnology and Bioengineering

Volumn 59, Issue 2, 1998, Pages 144-155

  Chang, Stephen T ^a   Fernandez, Erik J ^a  

^a University of Virginia   (United States)

Author keywords

Hydrogen exchange; Lysozyme; Nuclear magnetic resonance; Protein precipitation; Protein unfolding; Thiocyanate

Indexed keywords

CONFORMATIONS; DISSOLUTION; HYDROGEN; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH EFFECTS; PRECIPITATION (CHEMICAL); SULFUR COMPOUNDS;

LYSOZYME; PROTEIN UNFOLDING; THIOCYANATE;

ENZYME KINETICS;

LYSOZYME;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRECIPITATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

ANIMALS; CHICKENS; CHROMATOGRAPHY, GEL; EGG WHITE; FREEZE DRYING; MODELS, MOLECULAR; MURAMIDASE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; ULTRAFILTRATION;

EID: 0032551666     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980720)59:2<144::AID-BIT2>3.0.CO;2-H     Document Type: Article

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