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期刊论文
Further Investigation on Potassium-Induced Conformation Transition of Nephila Spidroin Film with Two-Dimensional Infrared Correlation Spectroscopy
Biomacromolecules, Vol. 6, No.1, 2005，-0001，（）：
We used two-dimensional (2D) correlation infrared spectroscopy to study further the potassium-induced conformation transition in Nephila spidroin films. It provided increased resolution and important new information on the sequence of events in the conformation transition process, showing that â-sheet formed from the helical component before they formed from random coil. It also showed more evidence that formation of the 1691cm-1 (turn/bend) peak did not proceed with the same kinetics as the 1620cm-1 (antiparallel â-sheet component) one, so we attribute the 1691cm-1 peak to turns which formed with different kinetics as the antiparallel β-sheets. We present a single coherent and detailed hypothesis for the assembly and secondary structural transition of silk proteins in vivo and in vitro based on our findings and on evidence from other laboratories.
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