Sökning: "oleic acid structure"
Visar resultat 1 - 5 av 17 avhandlingar innehållade orden oleic acid structure.
1. Lipid Self-Assembly and Lipase Action
Sammanfattning : In this thesis the action of the Thermomyces lanuginosa lipase (TLL) on "real" substrates, that is, lipid aggregates - vesicles, micelles, emulsions, gels and liquid crystals is discussed. Even for a pure triolein, the system becomes quite complex as the lipolytic process starts, both in terms of structure and composition, involving 5 additional components - diolein (DO), monoolein (MO), oleic acid (OA), sodium oleate (NaO) and glycerol . LÄS MER
2. Protein complexes : assembly, structure and function
Sammanfattning : Most proteins must fold into their native conformations to fulfil their biological functions. Failure of proteins to fold leads to cell pathology and a broad range of human diseases referred to as protein misfolding disease, e.g., Alzheimer’s disease, Parkinson’s disease, and type II diabetes. LÄS MER
3. Protein Complexity via Non-Native States: Binding, Stability, and Structural Studies of Calbindin D9k and HAMLET (Human alpha-lactalbumin Made LEthal to Tumor cells)
Sammanfattning : Using optical spectroscopy, nuclear magnetic resonance (NMR), and differential scanning Calorimetry (DSC), I have studied two different calcium binding proteins that can form kinetically trapped altered states. Calcium is very important in numerous biological processes such as blood coagulation, signal transduction, muscle contraction and bone formation. LÄS MER
4. Structure and stability of liposomes : Interactions with micelle- forming surfactants
Sammanfattning : The stability of phospholipid lipomes interacting with micelle-forming surfactants was studied under physiological conditions (150 mM NaCl and pH=7.4 unless otherwise stated) mainly by use of cryo-TEM and fluorescence. LÄS MER
5. Structure-function analysis of HAMLET (human alpha-lactalbumin made lethal to tumor cells)
Sammanfattning : The human genome sequence encodes fewer proteins than expected, suggesting that one protein can have several functions and adjust their structure to meet different structural demands. Changes in tertiary structure have mostly been associated with disease and the most striking example is the prion protein, which changes from a mixed alpha-helical and beta-sheet conformation to the beta-sheet rich, disease causing iso-form. LÄS MER