| Name | SANS |
|---|---|
| Synonyms | ANKS4A; SANS; Scaffold protein containing ankyrin repeats and SAM domain; Scaffold proteins containing ankyrin repeats and SAM domains; USH1G; Usher syndrome 1G (autosomal recessive); Usher syndrome type 1G protein; Scaffold protein containing ankyrin repeats and SAM domains… |
| Name | azobenzene |
|---|---|
| CAS | diphenyldiazene |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19715336 | Lee CT, Smith KA, Hatton TA: Small-Angle Neutron Scattering Study of the Micellization of Photosensitive Surfactants in Solution and in the Presence of a Hydrophobically Modified Polyelectrolyte (dagger). Langmuir. 2009 Aug 28. The self-assembly behavior of a light-sensitive azobenzene-based surfactant, both in pure surfactant solutions and in the presence of a hydrophobically modified, water-soluble polymer, has been investigated using small-angle neutron scattering (SANS), light scattering, and UV-vis absorption techniques. |
82(1,1,1,2) | Details |
| 19344185 | Hamill AC, Lee CT: Photocontrol of beta-amyloid peptide (1-40) fibril growth in the presence of a photosurfactant. J Phys Chem B. 2009 Apr 30;113(17):6164-72. The effect of an azobenzene-based photoresponsive surfactant on fibril formation of beta-amyloid (1-40) (Abeta40) has been studied using small-angle neutron scattering (SANS), atomic force microscopy (AFM), and light scattering (LS) measurements. |
7(0,0,1,2) | Details |
| 16460058 | Shang T, Smith KA, Hatton TA: Self-assembly of a nonionic photoresponsive surfactant under varying irradiation conditions: a small-angle neutron scattering and cryo-TEM study. Langmuir. 2006 Feb 14;22(4):1436-42. We have used small-angle neutron scattering (SANS), and cryogenic transmission electron microscopy (cryo-TEM) to determine the structure of aggregates formed by the photoresponsive surfactants diethylene glycol mono (4',4-butyloxy, butyl-azobenzene) (C4AzoOC4E2) and diethylene glycol mono (4',4-hexyloxy, butyl-azobenzene) (C4AzoOC6E2) under different illumination conditions. |
6(0,0,1,1) | Details |
| 18031062 | Wang SC, Lee CT Jr: Enhanced enzymatic activity through photoreversible conformational changes. Biochemistry. 2007 Dec 18;46(50):14557-66. Epub 2007 Nov 22. The cationic azobenzene surfactant undergoes a reversible photoisomerization upon exposure to the appropriate wavelength of light, with the visible-light (trans) form being more hydrophobic and, thus, inducing a greater degree of protein unfolding than the UV-light (cis) form. Conformational changes as a function of photoresponsive surfactant concentration and light illumination were measured through shape-reconstruction analysis of small-angle neutron scattering (SANS) data. |
3(0,0,0,3) | Details |
| 16285717 | Hamill AC, Wang SC, Lee CT Jr: Probing lysozyme conformation with light reveals a new folding intermediate. Biochemistry. 2005 Nov 22;44(46):15139-49. Upon exposure to the appropriate wavelength of light, the azobenzene surfactant undergoes a reversible photoisomerization, with the visible-light (trans) form being more hydrophobic than the UV-light (cis) form. Small-angle neutron scattering (SANS) measurements were used to provide detailed information of the protein conformation in solution. |
3(0,0,0,3) | Details |
| 15641777 | Lee CT Jr, Smith KA, Hatton TA: Photocontrol of protein folding: the interaction of photosensitive surfactants with bovine serum albumin. Biochemistry. 2005 Jan 18;44(2):524-36. The photoresponsive interaction of light-sensitive azobenzene surfactants with bovine serum albumin (BSA) at neutral pH has been investigated as a means to control protein folding with light irradiation. Small-angle neutron-scattering (SANS) measurements are used to provide detailed information on the protein conformation in solution. |
3(0,0,0,3) | Details |
| 16898769 | Wang SC, Lee CT Jr: Protein secondary structure controlled with light and photoresponsive surfactants. J Phys Chem B. 2006 Aug 17;110(32):16117-23. The interaction of a light-responsive azobenzene surfactant with bovine serum albumin (BSA) has been investigated as a means to examine photoreversible changes in protein secondary structure. Comparing the secondary structure changes induced by light illumination in the presence of the photoresponsive surfactant with previous measurements of the tertiary structure of BSA obtained from small-angle neutron scattering (SANS) allows the three discrete conformation changes in BSA to be fully characterized. |
2(0,0,0,2) | Details |