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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/47258

Title: Envelope Structure of Human eNOS Protein Revealed by Small-Angle X-ray Scattering
Authors: Chun-Yu Chen
Pei-Feng Chen
Yeukuang Hwu
U-Ser Jeng
Kun-Yu Wu
Keng S. Liang
Contributors: 國立臺灣海洋大學:光電科學研究所
Date: 2012-04
Issue Date: 2018-07-09T03:22:52Z
Abstract: Abstract: We investigate the solution structure of human eNOS protein by using synchrotron smallangle
X-ray scattering (SAXS). The pair-correlation analysis of the profile shows the radius
of gyration (Rg) and maxima dimension (Dmax) of 6.87 ± 0.03 nm and 22 nm, respectively.
The ratio of Dmax and Rg revealed that the protein was an extended conformation. The
ab initio shape determination and rigid-body calculations were performed to reconstruct
the real-space structure of eNOS in solution. The result shows that human eNOS form
homodimer form in solution with the closed contact of two oxygenase domains.
Relation: 50(2)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/47258
Appears in Collections:[光電科學研究所] 期刊論文

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