Thermodynamics of Substrate Binding to the Chaperone SecB †
✍ Scribed by Panse, Vikram G.; Swaminathan, Chittoor P.; Surolia, Avadhesha; Varadarajan, Raghavan
- Book ID
- 125981788
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 191 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Electrospray ionization mass spectrometry was used to investigate the structure of the __Escherichia coli__ chaperone protein SecB. It was determined that the N‐terminal methionine of SecB has been removed and that more than half of all SecB monomers are additionally modified, most like
The effect of polypeptide binding on the stability of the substrate binding domain of the molecular chaperone DnaK has been studied by thermodynamic analysis. The calorimetric scan of the fragment of the substrate binding domain DnaK384-638, consisting of a h-domain and an a-helical lid, showed two
## Abstract The chaperone protein SecB is dedicated to the facilitation of export of proteins from the cytoplasm to the periplasm and outer membrane of __Escherichia coli.__ It functions to bind and deliver precursors of exported proteins to the membrane‐associated translocation apparatus before th