Publications by authors named "Lisa A Della Ripa"
Article Synopsis
- Cholesterol is crucial for maintaining cell membrane structure and interacts with membrane proteins to regulate their function, making its structural dynamics important to understand.
- A new 3D solid-state NMR experiment has been developed to measure average dipolar couplings in cholesterol, offering insights into its molecular behavior.
- The findings indicate that the dynamics of cholesterol's structure—like ring tilt and tail conformation changes—are interconnected, which could help explain how such small molecules influence biological functions.
Cholesterol (Chol) is vital for cell function as it is essential to a myriad of biochemical and biophysical processes. The atomistic details of Chol's interactions with phospholipids and proteins is therefore of fundamental interest, and NMR offers unique opportunities to interrogate these properties at high resolution. Towards this end, here we describe approaches for examining the structure and dynamics of Chol in lipid bilayers using high levels of C enrichment in combination with magic-angle spinning (MAS) methods.
View Article and Find Full Text PDFAmphotericin B (AmB) is the archetype for small molecules that form ion channels in living systems and has recently been shown to replace a missing protein ion transporter and thereby restore physiology in yeast. Molecular modeling studies predict that AmB self-assembles in lipid membranes with the polyol region lining a channel interior that funnels to its narrowest region at the C3-hydroxyl group. This model predicts that modification of this functional group would alter conductance of the AmB ion channel.
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