Influence of Detergent and Lipid Composition on Reconstituted Membrane Proteins for Structural Studies

Lipid composition in cellular membranes plays an important role in maintaining the structural integrity of cells and in regulating cellular signaling that controls functions of both membrane-anchored and cytoplasmic proteins. ATP-dependent ABC and P4-ATPase lipid transporters, two integral membrane proteins, are known to contribute to lipid translocation across the lipid bilayers on the cellular membranes. In this review, we will highlight current knowledge about the role of cholesterol and phospholipids of cellular membranes in regulating cell signaling and how lipid transporters participate this process.

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Triton X-100-4 M urea as an extraction medium for membrane proteins. II. Molecular properties of pure cytochrome b559. Lipoprotein containing small polypeptide chains and a limited lipid composition

Biochemistry ◽

10.1021/bi00717a002 ◽

1974 ◽

Vol 13 (20) ◽

pp. 4072-4079 ◽

Cited By ~ 29

Author(s):

Harinder S. Garewal ◽

Aaron R. Wasserman

Keyword(s):

Membrane Proteins ◽

Lipid Composition ◽

Molecular Properties ◽

Cytochrome B559 ◽

Small Polypeptide ◽

Triton X ◽

Polypeptide Chains

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Detergent-free extraction, reconstitution and characterization of membrane-anchored cytochrome-b5 in native lipids

Chemical Communications ◽

10.1039/d0cc01737j ◽

2020 ◽

Vol 56 (48) ◽

pp. 6511-6514 ◽

Cited By ~ 1

Author(s):

Bankala Krishnarjuna ◽

Thirupathi Ravula ◽

Ayyalusamy Ramamoorthy

Keyword(s):

High Resolution ◽

Membrane Proteins ◽

Cytochrome B5 ◽

Target Protein ◽

Structural Studies ◽

Net Charge

Directly extracted membrane proteins are stable and suitable for functional and high-resolution structural studies; however, the efficacy is modulated by the net charge of the target protein and the polymer used at a given pH.

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Structural Studies of Membrane Proteins using Pulsed EPR Spectroscopy

Biophysical Journal ◽

10.1016/j.bpj.2018.11.345 ◽

2019 ◽

Vol 116 (3) ◽

pp. 56a

Author(s):

Gary A. Lorigan ◽

Indra D. Sahu ◽

Daniel L. Drew ◽

Gunjan Dixit ◽

Tanbir Ahammad

Keyword(s):

Membrane Proteins ◽

Epr Spectroscopy ◽

Structural Studies ◽

Pulsed Epr

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NMR Structural Studies of Antimicrobial Peptides as In-Plane Helix of Membrane Proteins

Biophysical Journal ◽

10.1016/j.bpj.2013.11.1140 ◽

2014 ◽

Vol 106 (2) ◽

pp. 192a-193a ◽

Cited By ~ 1

Author(s):

Yongae Kim ◽

Ji-Ho Jeong ◽

Ji-Sun Kim

Keyword(s):

Membrane Proteins ◽

Antimicrobial Peptides ◽

Structural Studies

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Circular Dichroism Analysis of Native and Reaggregated Mycoplasma Membranes

Canadian Journal of Biochemistry ◽

10.1139/o73-079 ◽

1973 ◽

Vol 51 (5) ◽

pp. 632-636 ◽

Cited By ~ 6

Author(s):

Shlomo Rottem ◽

Leonard Hayflick

Keyword(s):

Circular Dichroism ◽

Membrane Proteins ◽

Sodium Dodecyl Sulfate ◽

Lipid Composition ◽

Sodium Dodecyl ◽

Growth Cycle ◽

Membrane Material ◽

Α Helix ◽

Low Amplitude ◽

Circular Dichroïsm

Circular dichroism analyses of Acholeplasma laidlawii membranes solubilized by sodium dodecyl sulfate showed a typical α-helix spectrum. The estimated α-helix content was of the order of 35% calculated from the ellipticity at 208 nm of membranes solubilized by 20 mM SDS. Reaggregation of the solubilized membrane material to a membrane-like structure resulted in a distorted spectrum with low amplitude and red-shifted extrema like that of the native membranes. Throughout the growth cycle the circular dichroism spectra of membrane proteins remained the same despite the marked differences in membrane densities. The optical activity of the membranes was not affected by changing the lipid composition or extraction of over 90% of the lipids, although the latter resulted in marked destabilization of the proteins.

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