Envelope Structure of Human eNOS Protein Revealed by Small-Angle X-ray Scattering
| dc.citation.epage | 344 | en_US |
| dc.citation.issue | 2 | en_US |
| dc.citation.volume | 50 | en_US |
| dc.citation.woscount | 1 | |
| dc.contributor.author | Chen, Chun-Yu | en_US |
| dc.contributor.author | Chen, Pei-Feng | en_US |
| dc.contributor.author | Hwu, Yeukuang | en_US |
| dc.contributor.author | Jeng, U-Ser | en_US |
| dc.contributor.author | Wu, Kun-Yu | en_US |
| dc.contributor.author | Liang, Keng S. | en_US |
| dc.contributor.department | 電子物理學系 | zh_TW |
| dc.contributor.department | Department of Electrophysics | en_US |
| dc.date.accessioned | 2014-12-08T15:23:18Z | |
| dc.date.available | 2014-12-08T15:23:18Z | |
| dc.date.issued | 2012-04-01 | en_US |
| dc.description.abstract | We investigate the solution structure of human eNOS protein by using synchrotron small-angle X-ray scattering (SAXS). The pair-correlation analysis of the profile shows the radius of gyration (R-g) and maxima dimension (D-max) of 6.87 +/- 0.03 nm and 22 nm, respectively. The ratio of D-max and R-g 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. | en_US |
| dc.identifier.issn | 0577-9073 | en_US |
| dc.identifier.journal | CHINESE JOURNAL OF PHYSICS | en_US |
| dc.identifier.uri | https://ir.lib.nycu.edu.tw/handle/11536/16350 | |
| dc.identifier.wosnumber | WOS:000304060000020 | |
| dc.language.iso | en_US | en_US |
| dc.title | Envelope Structure of Human eNOS Protein Revealed by Small-Angle X-ray Scattering | en_US |
| dc.type | Article | en_US |