引用本文:
Tong Kuan XU, Xing Hai SHEN, Na LI, Hong Cheng GAO. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin[J]. Chinese Chemical Letters,
2005, 16(7): 943-946.
Citation: Tong Kuan XU, Xing Hai SHEN, Na LI, Hong Cheng GAO. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin[J]. Chinese Chemical Letters, 2005, 16(7): 943-946.
Citation: Tong Kuan XU, Xing Hai SHEN, Na LI, Hong Cheng GAO. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin[J]. Chinese Chemical Letters, 2005, 16(7): 943-946.
Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin
摘要:
The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Forster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher,and the distance between tryptophan and 3H-indole is nearer.
English
Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin
Abstract:
The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Forster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher,and the distance between tryptophan and 3H-indole is nearer.
扫一扫看文章
计量
- PDF下载量: 0
- 文章访问数: 0
- HTML全文浏览量: 0
下载:
