The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes
نویسندگان
چکیده
منابع مشابه
The gross conformation of protein-sodium dodecyl sulfate complexes.
The interaction of sodium dodecyl sulfate with a wide variety of proteins is characterized by a high binding ratio when the monomer concentration of amphiphile exceeds 5 x 10W4 M. This binding ratio on a gram to gram basis is identical for all proteins investigated. The protein portion of the complex contains a high degree of order, and hydrodynamic studies suggest that the complex is a rodlike...
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Reduced and unreduced lysozyme aggregates formed by formaldehyde cross-linking comprise a set of model compounds for studying the effects of protein conformation on the electrophoretic mobilities of sodium dodecyl sulphate-protein complexes. The reduced aggregates were indistinguisable from normal proteins, but the unreduced aggregates migrated anomalously fast by about 14%. Contrary to expecta...
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The structure of lysozyme-sodium dodecyl sulfate (SDS) complexes in solution is studied using small-angle X-ray scattering (SAXS). The SAXS data cannot be explained by the necklace and bead model for unfolded polypeptide chain interspersed with surfactant micelles. For the protein and surfactant concentrations used in the study, there is only marginal growth of SDS micelles as they complex with...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62831-5