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• W1489280123 abstract "To summarize recent advances towards an understanding of the three-dimensional structures of the apolipoprotein components of HDL with a specific focus on high resolution models of apolipoprotein A-I.Since the primary sequence was first reported, various models have been advanced for the structure of apolipoprotein A-I, the major protein constituent of HDL, in its lipid-free and lipid-bound forms. Unfortunately, the generation of experimental data capable of distinguishing among the competing models has lagged far behind. However, recent experimental strategies, including X-ray crystallography, applications of resonance energy transfer and mass spectrometry, have combined with sophisticated theoretical approaches to develop three-dimensional structural models of apolipoprotein A-I with previously unavailable resolution.The recent synergy of sophisticated computer modeling techniques with hard experimental data has generated new models for apolipoprotein A-I in certain subclasses of HDL produced in vitro. The challenge now is to adapt and test these models in the more complex forms of HDL isolated directly from human plasma." @default.
• W1489280123 created "2016-06-24" @default.
• W1489280123 creator A5008316828 @default.
• W1489280123 creator A5043923168 @default.
• W1489280123 date "2005-06-01" @default.
• W1489280123 modified "2023-09-27" @default.
• W1489280123 title "Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins" @default.
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• W1489280123 doi "https://doi.org/10.1097/01.mol.0000169349.38321.ad" @default.
• W1489280123 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15891390" @default.
• W1489280123 hasPublicationYear "2005" @default.
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