Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Sodium Dodecyl Sulfate/*chemistry"'
Autor:
Sampson Anankanbil, Guoqin Liu, Jacob Nedergaard Pedersen, Bianca Pérez, Zheng Guo, Weiwei Cheng
Publikováno v:
Cheng, W, Anankanbil, S, Pérez, B, Pedersen, J N, Liu, G & Guo, Z 2019, ' Aspartic-acid-based ampholytic amphiphiles: Synthesis, characterization, and pH-dependent properties at air/water and oil/water interfaces ', Journal of Agricultural and Food Chemistry, vol. 67, no. 8, pp. 2321-2330 . https://doi.org/10.1021/acs.jafc.8b05122
A facile and two-step strategy was employed to synthesize a series of novel aspartic-acid-based ampholytic amphiphiles from sustainable and commercially viable substances as starting materials. The molecular structures of the synthetic compounds were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c5fd9eb7941d82eead548e998c28b1d
https://doi.org/10.1021/acs.jafc.8b05122
https://doi.org/10.1021/acs.jafc.8b05122
Autor:
Yang, Shenyu, Yan, Yun, Huang, Jianbin, Petukhov, Andrei V., Kroon - Batenburg, Loes M. J., Drechsler, Markus, Zhou, Chengcheng, Tu, Mei, Granick, Steve, Jiang, Lingxiang, Sub Physical and Colloid Chemistry, Sub Crystal and Structural Chemistry, Physical and Colloid Chemistry, Crystal and Structural Chemistry
Publikováno v:
Nature Communications, 8:15856, 1-7. Nature Publishing Group
'Nature Communications ', vol: 8, pages: 15856-1-15856-17 (2017)
Nature Communications, 8. Nature Publishing Group
Nature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
Nature Communications
'Nature Communications ', vol: 8, pages: 15856-1-15856-17 (2017)
Nature Communications, 8. Nature Publishing Group
Nature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
Nature Communications
Proteins can readily assemble into rigid, crystalline and functional structures such as viral capsids and bacterial compartments. Despite ongoing advances, it is still a fundamental challenge to design and synthesize protein-mimetic molecules to form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d03ab53e933e90da46a3c7d3bef1dbec
https://doi.org/10.1038/ncomms15856
https://doi.org/10.1038/ncomms15856
Publikováno v:
Leon, I R, Schwämmle, V, Jensen, O N & Sprenger, R R 2013, ' Quantitative assessment of in-solution digestion efficiency identifies optimal protocols for unbiased protein analysis : Quantitative assessment of protein digestion protocols ', Molecular and Cellular Proteomics, vol. 12, no. 10, pp. 2992-3005 . https://doi.org/10.1074/mcp.M112.025585
The majority of mass spectrometry-based protein quantification studies uses peptide-centric analytical methods and thus strongly relies on efficient and unbiased protein digestion protocols for sample preparation. We present a novel objective approac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3062::91fb0a22a8c3bdff71051ca624dea350
https://portal.findresearcher.sdu.dk/da/publications/c0ee5019-ff4f-49b7-b8ab-dfa2f072f743
https://portal.findresearcher.sdu.dk/da/publications/c0ee5019-ff4f-49b7-b8ab-dfa2f072f743
Publikováno v:
European Journal of Pharmaceutical Sciences, Vol. 15, No 2 (2002) pp. 225-234
The rational use of micelles in quantitative structure-activity and quantitative structure-permeation relationships implies a good knowledge of the nature of recognition forces underlying solute-micelle association. The aims of this study were to unr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee841c45e10ef1dff34efcfa55178cfd
https://pubmed.ncbi.nlm.nih.gov/11849920
https://pubmed.ncbi.nlm.nih.gov/11849920
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