SecB-A chaperone dedicated to protein translocationBechtluft, P., Nouwen, N., Tans, S. J. & Driessen, A. J. M., 2010, In : Molecular BioSystems. 6, 4, p. 620-627 8 p.
Research output: Contribution to journal › Review article › Academic › peer-review
SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.
|Number of pages||8|
|Publication status||Published - 2010|
- MALTOSE-BINDING PROTEIN, BACTERIAL CYTOPLASMIC MEMBRANE, ESCHERICHIA-COLI, SIGNAL SEQUENCE, ANTIFOLDING ACTIVITY, DENATURED PROTEINS, SUBSTRATE PROTEIN, CRYSTAL-STRUCTURE, FOLDING PATHWAY, TRIGGER FACTOR