Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
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Summary
It is shown that for a mixture of proteins refolding in vitro, folding intermediates do not coaggregate with each other but only with themselves, which indicates that aggregation occurs by specific interaction of certain conformations of folding intermediate rather than by nonspecific coaggregation, providing a rationale for recovering relatively pure protein from the inclusion body state.
- Type
- article
- Published
- 1996-10-01
- Cited by
- 323
- References
- 42
- OpenAlex
- https://openalex.org/W1980597219
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36883690
Keywords
Folding (DSP implementation), Chemistry, Protein folding, Inclusion bodies, Protein aggregation
References
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Cited by
- Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography
- In situ proteolytic digestion of inclusion body polypeptides occurs as a cascade process.
- Analysis of Molecular Interactions in Heat-induced Aggregation of a Non-inhibitory Serpin Ovalbumin Using a Molecular Chaperone
- Confocal spectrofluorimetric evidence for the hetero-aggregation of sequence-scrambled forms of two model all-beta sheet proteins.
- Kinetics of Inclusion Body Formation and Its Correlation with the Characteristics of Protein Aggregates in Escherichia coli
- Folate binding protein in bovine milk
- Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli.
- Effects of Osmolytes on Unfolding of Chicken Liver Fatty Acid Synthase
- Protein aggregation from inclusion bodies to amyloid and biomaterials.
- Intrinsic Fluorescence of Actin
- Dynamic control of protein conformation transition in chromatographic separation based on hydrophobic interactions: molecular dynamics simulation.
- Physical stabilization of proteins in aqueous solution.
- Protein aggregation as a cause for disease.
- Recombinant production of native proteins from Escherichia coli.
- Mycobacterium tuberculosis complex-specific antigens for use in serodiagnosis of bovine tuberculosis
- Immobilisation of active enzymes on novel GFP protein particles : a thesis submitted in complete fulfilment of the requirements of the degree of Master of Science in Microbiology at Massey University, Palmerston North, New Zealand
- Isolation, solubilization, refolding, and chromatographic purification of human growth hormone from inclusion bodies of Escherichia coli cells: a case study.
- Characterization of Antigenic Properties and High Throughput Protein Purification
- Investigation into the structure and function of Hsp47
- Osmolyte Effects on the Unfolding Pathway of β -Lactoglobulin
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