2008
DOI: 10.1016/j.jcis.2008.09.012
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A small-angle X-ray scattering study of the structure of lysozyme–sodium dodecyl sulfate complexes

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Cited by 23 publications
(22 citation statements)
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References 43 publications
(68 reference statements)
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“…In contrast with the work of Narayanan et al, [22] the SAXS data presented for the 50 mM SDS sample in this work show an additional upturn in the SAXS at q < 0.25 nm…”
Section: Resultscontrasting
confidence: 99%
See 1 more Smart Citation
“…In contrast with the work of Narayanan et al, [22] the SAXS data presented for the 50 mM SDS sample in this work show an additional upturn in the SAXS at q < 0.25 nm…”
Section: Resultscontrasting
confidence: 99%
“…The SAXS curve obtained for the pure SDS sample is qualitatively similar to that reported by Narayanan et al for a 70 mM SDS solution in water. [22] Their scattering curves were modelled assuming that the micelles adopt a prolate ellipsoidal shape of ca. 3.3 2.3 nm with a core-shell type morphology in which the electron density of the core (composed of the hydrocarbon chains) is less than that of water and that the shell (composed of the SDS head groups; 0.65 nm thick) has a greater electron density than the solvent.…”
Section: Resultsmentioning
confidence: 99%
“…Interestingly, α of PCN1 and PCN2 nanofibers is calculated to be 3 and 4, respectively (Table ), from Porod's law ( I ( q )∝ q −3 or q −4 ) and suggested a nonfractal structure that has even interfaces. However, the slope of the data of PCN0 and PCN5 (Figure c) is 3.5 and 3.4, respectively, which corresponds to a surface fractal structure that has dimensions ( D s ) of 2.5 and 2.6 ( α =6− K s ) . In summary, the SAXS results agree with the observed nanofiber micrographs and suggested the possibility of a high charge transfer in PCN1 nanofibers during electrochemical reactions.…”
Section: Resultssupporting
confidence: 76%
“…These studies indicate that complex formation is driven by electrostatic interactions as well as interactions between exposed hydrophobic patches on the unfolded protein and the surfactant micelles. Other studies of lysozyme (16,17), a-lactalbumin (18), and Acyl-CoAbinding protein (ACBP) (19) with SDS added in different proportions, highlight a variety of complex structures with increasing SDS concentration. At low SDS concentrations, the native ACBP binds a small number of SDS molecules, whereas intermediate SDS concentrations lead to a protein dimer formed around a shared micelle; finally, higher SDS concentrations lead to complexes with only one protein per micelle.…”
Section: Introductionmentioning
confidence: 99%