Effect of temperature on self-assembly of bovine beta-casein above and below isoelectric pH. Structural analysis by cryogenic-transmission electron microscopy and small-angle X-ray scattering
beta-Casein is one of the main proteins in milk, recently classified as an intrinsically unstructured protein. At neutral pH, it is composed of a highly polar N-terminus domain and a hydrophobic C-terminus tail. This amphiphilic block-copolymer-like structure leads to self-organization of the protei...
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Bibliographische Detailangaben
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 24(2008), 7 vom: 01. Apr., Seite 3020-9
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| 1. Verfasser: |
Moitzi, Christian
(VerfasserIn) |
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| Weitere Verfasser: |
Portnaya, Irina,
Glatter, Otto,
Ramon, Ory,
Danino, Dganit |
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| Format: | Online-Aufsatz
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| Sprache: | English |
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| Veröffentlicht: |
2008
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids
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| Schlagworte: | Journal Article
Research Support, Non-U.S. Gov't
Caseins |
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