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Direct Observation of Chaperone-Induced Changes in a Protein Folding Pathway
- Source :
- Science, 318(5855), 1458-1461. AMER ASSOC ADVANCEMENT SCIENCE
- Publication Year :
- 2007
- Publisher :
- American Association for the Advancement of Science (AAAS), 2007.
-
Abstract
- How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several α helices are finally wrapped. Interactions with SecB completely prevent stable tertiary contacts in the core structure but have no detectable effect on the folding of the external α helices. It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions.
- Subjects :
- Models, Molecular
Protein Folding
SECB
Optical Tweezers
Protein Conformation
SUBSTRATE PROTEIN
Peptide
Protein Structure, Secondary
Molecular dynamics
Maltose-binding protein
Protein structure
Bacterial Proteins
Computer Simulation
PEPTIDE
MOLECULE
ATOMIC-FORCE MICROSCOPY
chemistry.chemical_classification
Multidisciplinary
biology
Escherichia coli Proteins
Binding protein
TERTIARY STRUCTURE
MALTOSE-BINDING PROTEIN
EXPORT
Protein tertiary structure
Protein Structure, Tertiary
TRANSLOCATION
chemistry
Biochemistry
Periplasmic Binding Proteins
Chaperone (protein)
biology.protein
Biophysics
Protein folding
MEMBRANE
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 318
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....5c939d3e8004a6d6a57b927b3d0ec346
- Full Text :
- https://doi.org/10.1126/science.1144972