First Advisor

Drake C. Mitchell

Date of Publication

12-20-2018

Document Type

Thesis

Degree Name

Master of Science (M.S.) in Physics

Department

Physics

Language

English

Subjects

Copolymers, Solubilization, Membranes (Biology)

DOI

10.15760/etd.6719

Physical Description

1 online resource (vii, 73 pages)

Abstract

Cell membranes, or plasma membranes, play an essential role in the structure and the function of living cells. In 1972, the fluid mosaic membrane model was the first unifying paradigm of membrane structure. It is no longer considered adequate because evidence of many non-homogeneous lipid structures in both natural and model membranes have been discovered over the past thirty years. The field of membrane biophysics now uses updated versions of the mosaic model, which consists of the complex mixture of different lipid species. The lipid species found in natural membranes produce a range of dynamic, laterally segregated, non-homogeneous domains, which exist on time scales ranging from microseconds to minutes. The cell membrane is an enclosing or separating membrane that acts as a selectively permeable barrier within living things. It consists of the phospholipid bilayer with associated embedded proteins, integral (intrinsic) and peripheral (extrinsic) proteins used for various biological activities. Proteins, especially integral membrane proteins, perform a range of key functions vital to the cell, such as controlled movement of molecules across lipid bilayers, as well as participating in cell signaling and motility. The major obstacle to studying membrane proteins is the tendency for some of their properties to change and the proteins themselves may be denatured when extracted by detergents. One of the most significant approaches to solve this problem is the use of styrene-maleic acid copolymers (SMAs), which offers detergent-free solubilization of embrane, which allows studies of membrane proteins to be done in very small systems. The main goal of this thesis is to examine the effects of these polymers on the interior of the lipid bilayer. With these, membrane proteins can be extracted from cell membranes while conserving a patch of near-native membrane around them. It has been suggested but not proven that proteins in nanodiscs reside in a hydrophobic environment that is identical to that found in the native cell membrane. Moreover, I also investigate the kinetics of membrane solubilization by SMA by using UV/visible spectrophotometer. In addition, I examine how lipid packing in the nanodiscs is affected by the presence of the polymers and how it depends on polymer composition by using SMA variants with different styrene-to-maleic acid ratios.

Rights

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Persistent Identifier

https://archives.pdx.edu/ds/psu/28341

Included in

Biophysics Commons

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