Journal
BIOMACROMOLECULES
Volume 15, Issue 12, Pages 4447-4454Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm501241n
Keywords
-
Funding
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Fonds de recherche du Quebec - Nature et Technologies (FRQ-NT)
- Regroupement quebecois de recherche sur la structure, la fonction et l'ingenierie des proteines (PROTEO)
- Centre de recherche sur les materiaux avances (CERMA)
- Centre quebecois sur les materiaux fonctionnels (CQMF)
- NSERC
- FRQ-NT
Ask authors/readers for more resources
Spider silk proteins undergo a complex series of molecular events before being converted into an outstanding hierarchically organized fiber. Recent literature has underlined the crucial role of the C-terminal domain in silk protein stability and fiber formation. However, the effect of pH remains to be clarified. We have thus developed an efficient purification protocol to obtain stable native-like recombinant MaSp1 C-terminal domain of Nephila clavipes (NCCTD). Its structure was investigated as a function of pH using circular dichroism, fluorescence and solution NMR spectroscopy. The results show that the NCCTD structure is very sensitive to pH and suggest that a molten globule state occurs at pH 5.0 and below. Electronic microscopy images also indicate fiber formation at low pH and coarser globular particles at more basic pH. The results are consistent with a spinning process model where the NCCTD acts as an aggregation nucleus favoring the b-aggregation of the hydrophobic polyalanine repeats upon spinning.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available