Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein

Protein Science

Volumn 10, Issue 8, 2001, Pages 1635-1644

  Ganesh, C ^a,d   Zaidi, Faisal N ^b   Udgaonkar, Jayant B ^b   Varadarajan, Raghavan ^a,c  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^c JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Aggregation; Folding; Intermediates; MBP

Indexed keywords

CHAPERONE; MALTOSE BINDING PROTEIN;

ARTICLE; ESCHERICHIA COLI; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE;

ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; CARRIER PROTEINS; CIRCULAR DICHROISM; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANIDINE; KINETICS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; MONOSACCHARIDE TRANSPORT PROTEINS; PRECIPITATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

ESCHERICHIA COLI;

EID: 0034913646     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8101     Document Type: Article

References (38)

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11. Pole cap formation in Escherichia coli following induction of the maltose-binding protein
12. Commitment to folded and aggregated states occurs late in interleukin-1β folding
13. Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1β
14. Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein
15. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein
16. The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
17. Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export
18. Thermodynamics of model prions and its implications for the problem of priori protein folding
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20. In vitro synthesis of "amyloid" fibrils from insulin, calcitonin and parathormone
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27. SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state
28. Occurrence of transient multimeric species during the refolding of a monomeric protein
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30. Refolding of denatured and denatured/reduced lysozyme at high concentrations
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32. Transient aggregates in protein folding are easily mistaken for folding intermediates
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34. Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
35. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
36. Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli. Influence of folding catalysts
37. Control of aggregation in protein refolding: The temperature-leap tactic