POLYMER INDUCED CONFORMATIONAL TRANSITION OF PROTEIN IN SILK FIBROIN AS REVEALED BY COMBINED SOLID-STATE NMR AND FIRST PRINCIPLES CALCULATIONS
Proteins are an important class of biological macromolecules present in all biological organisms, and the ability of a special protein to exercise its functions is usually caused by its conformation. Growing number of studies have shown that many process of life activities are closely related to the changes of protein conformation. The studies of animal protein fiber have shown that excellent mechanical properties of silk worm and spider silk is closely related to its conformation. The p-sheet structure is related to the fiber strength while random coil structure is related to the flexibility of the protein fibers.1 Therefore, study of the protein conformation and the conformational transition are of great significance. Poly(ethylene glycol) (PEG) is known to play a vital role in controlling conformational changes of proteins, because it can strongly affect the properties and structure of water surrounding the proteins. 2 Nevertheless, the underlying mechanisms, including conformational changes of proteins and the specific interaction between PEG and protein are still poorly understood and need to be further elucidated.3 In the present work, we aim to elucidate the effect of PEG on the high P-sheet transition of silk fibroin (SF) and the specific interaction of different components in SF/PEG blends cast under different temperature by using advanced solid-state NMR (SSNMR) and first principles calculations.
Qinqin Dang Yuzhu Chen Shen Yu Pinechuan Sun ZhiYuan
Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry and College of Chemistry, Nankai University, Tianjin 300071, China
国际会议
PP’2010，Jinan International Symposium on Polymer Physics(2010济南国际高分子物理学术研讨会)
济南
英文
205-206
2010-06-06（万方平台首次上网日期，不代表论文的发表时间）