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- W1598788587 abstract "Publisher Summary The dominant structural motif of the peripheral apolipoproteins is the amphipathic helix, which is responsible for the reversible association of these proteins with lipids, as well as for many biological functions mediated by these apolipoproteins. This chapter reviews the different classes of amphipathic helices, using a combination of powerful computer programs to develop a comparison database and to analyze these structures. It also discusses their evolutionary origins, physical-chemical properties, X-ray structure determination, and conformational analysis. Although the structures of these lipoprotein classes are similar, they differ in relative proportion of lipids, in the apolipoprotein: lipid ratio and in the apolipoprotein species. The amphipathic α helix plays a pivotal role in the structure and functions of the exchangeable apolipoproteins. Site-directed mutagenesis and other molecular biology-based techniques are available for probing the structural motif. The location and properties of the amphipathic helices in apolipoproteins and the results are compared with recently developed and ever-expanding computer methods for the location and characterization. A variety of structure-function studies, including the activation of lipoprotein lipase, receptor recognition, lecithin-cholesterol acyltransferase (LCAT) activation, and antiviral and anti-inflammatory activities are also discussed." @default.
- W1598788587 created "2016-06-24" @default.
- W1598788587 creator A5008080313 @default.
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- W1598788587 creator A5062920055 @default.
- W1598788587 creator A5088307660 @default.
- W1598788587 creator A5090384781 @default.
- W1598788587 date "1994-01-01" @default.
- W1598788587 modified "2023-09-30" @default.
- W1598788587 title "The Amphipathic α Helix: A Multifunctional Structural Motif in Plasma Apolipoproteins" @default.
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