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Fluorescence characterization of the thermal stability of collagen mimic peptides
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作者 Xiu-Xia Sun Jun Fan +3 位作者 Yan-Nan Hou Shuo Liang Yu-Ping Zhang jian-xi xiao 《Chinese Chemical Letters》 SCIE CAS CSCD 2017年第5期963-967,共5页
The thermal stability of triple helical structure plays a critical role in collagen biosynthesis,function and degradation.CD technique was utilized to characterize the thermal stability of synthetic collagen mimic pep... The thermal stability of triple helical structure plays a critical role in collagen biosynthesis,function and degradation.CD technique was utilized to characterize the thermal stability of synthetic collagen mimic peptides.Fluorescence spectroscopy is widely used with easy access all around the world because of its inexpensive instrumentation,low operation cost,easy operation,and high sensitivity.Here we have developed an alternative fluorescence method to detect the thermal stability of collagen mimic peptides.We have demonstrated that fluorescence spectroscopy could measure the thermal stability of collagen mimic peptides with low concentrations under different circumstances.This highly sensitive fluorescence self-quenching assay will greatly expedite the studies of sequence-dependent properties of collagen mimic peptides,and it has great potential in the application of determining the thermal stability of triple helix systems such as collagens,collectins,adiponectin,macrophage scavenger and C1q. 展开更多
关键词 Collagen Peptides Thermal stability Fluorescence Triple helix
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