Atomic-level characterization of protein-lipid interactions using molecular dynamics simulations

Peripheral membrane proteins are structurally diverse proteins that are involved in fundamental cellular processes. Their activity of these proteins is frequently modulated through their interaction with cellular membranes, and as a result techniques to study the interfacial interaction between peripheral proteins and the membrane are in high demand. Due to the fluid nature of the membrane and the reversibility of protein–membrane interactions, the experimental study of these systems remains a challenging task. Molecular dynamics (MD) simulations offer a suitable approach to study protein–lipid interactions with high spatial and temporal resolution. Here, we present a summary of recent applications of MD simulations to study the interaction of different classes of membrane proteins with lipid bilayers at the atomic level. Specific systems studied include membrane-bound cytochrome P450 (CYP) enzymes, a class membrane proteins involved in the metabolism of a wide range of molecules, the hemagglutinin fusion peptide (HAfp), a small peptide that mediates the fusion process of the influenza virus to a host cell, and the T-cell immunoglobulin and mucin domain (Tim) proteins, involved in the mechanism of lipid recognition by T-cells.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics & Computnl Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2016

Author dc:creator

• Baylon Cardiel, Javier Lorenzo

Contributors dc:contributor

• Tajkhorshid, Emad
• Gennis, Robert B.
• Rienstra, Chad
• Schuler, Mary

• Membrane
• Peripheral proteins
• Molecular dynamics
• Lipids

Statement dc:rights

• Copyright 2016 Javier Baylon Cardiel

Language dc:language

en

Handle dc:identifier

http://hdl.handle.net/2142/92708

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/92708