Effect of rate of chemical or thermal renaturation on refolding and aggregation of a simple lattice protein

Biotechnology and Bioengineering

Volumn 80, Issue 7, 2002, Pages 823-834

  Nguyen, Hung D ^a   Hall, Carol K ^a  

^a North Carolina State University   (United States)

Author keywords

Computer simulation; Monte Carlo; Protein aggregation; Protein folding; Renaturation

Indexed keywords

AGGLOMERATION; FILTRATION; MONTE CARLO METHODS; PROTEINS; QUENCHING;

LOW REFOLDING YIELDS; THERMAL RENATURATION;

BIOTECHNOLOGY;

PROTEIN;

ARTICLE; CHEMICAL REACTION; COMPUTER SIMULATION; COOLING; DIAFILTRATION; DIALYSIS; DILUTION; MONTE CARLO METHOD; NONPHOTOCHEMICAL QUENCHING; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN RENATURATION; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; EVALUATION; MACROMOLECULE; PROTEIN CONFORMATION; SENSITIVITY AND SPECIFICITY; TEMPERATURE;

COMPUTER SIMULATION; MACROMOLECULAR SUBSTANCES; MODELS, CHEMICAL; MODELS, MOLECULAR; MONTE CARLO METHOD; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEINS; SENSITIVITY AND SPECIFICITY; TEMPERATURE;

EID: 0037203044     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10448     Document Type: Article

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