Structure and Function of Membrane Proteins

2021 ◽  
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
And Function

How Do Lipids Affect the Structure and Function of Integral Membrane Proteins

2012 ◽  
Vol 28 (11) ◽  
pp. 866
Author(s):  
Jie HENG ◽  
Yan WU ◽  
Xianping WANG ◽  
Kai ZHANG
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
Integral Membrane Proteins ◽  
And Function

Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function

2017 ◽  
Vol 6 (1) ◽  
pp. 75-92 ◽  
Author(s):  
Elka R. Georgieva
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Spin Labeling ◽  
Structure And Function ◽  
Protein Structure And Function ◽  
Paramagnetic Resonance ◽  
And Function ◽  
Electron Paramagnetic

AbstractCellular membranes and associated proteins play critical physiological roles in organisms from all life kingdoms. In many cases, malfunction of biological membranes triggered by changes in the lipid bilayer properties or membrane protein functional abnormalities lead to severe diseases. To understand in detail the processes that govern the life of cells and to control diseases, one of the major tasks in biological sciences is to learn how the membrane proteins function. To do so, a variety of biochemical and biophysical approaches have been used in molecular studies of membrane protein structure and function on the nanoscale. This review focuses on electron paramagnetic resonance with site-directed nitroxide spin-labeling (SDSL EPR), which is a rapidly expanding and powerful technique reporting on the local protein/spin-label dynamics and on large functionally important structural rearrangements. On the other hand, adequate to nanoscale study membrane mimetics have been developed and used in conjunction with SDSL EPR. Primarily, these mimetics include various liposomes, bicelles, and nanodiscs. This review provides a basic description of the EPR methods, continuous-wave and pulse, applied to spin-labeled proteins, and highlights several representative applications of EPR to liposome-, bicelle-, or nanodisc-reconstituted membrane proteins.

scholarly journals Bioinformatic approaches for the structure and function of membrane proteins

BMB Reports ◽  
2009 ◽  
Vol 42 (11) ◽  
pp. 697-704 ◽  
Author(s):  
Hyun-Jun Nam ◽  
Jou-Hyun Jeon ◽  
Sang-Uk Kim
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
Bioinformatic Approaches ◽  
And Function

Structure and function of qiuinone binding membrane proteins

2003 ◽  
pp. 151-176 ◽  
Author(s):  
Momi Iwata ◽  
Jeff Abramson ◽  
Bernadette Byrne ◽  
S.O Iwata
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
And Function

Biophysical methods toolbox to study ABC exporter structure and function

2017 ◽  
Vol 398 (2) ◽  
pp. 229-235
Author(s):  
Thomas Marcellino ◽  
Vasundara Srinivasan
Keyword(s):  
Membrane Proteins ◽  
Abc Transporter ◽  
Integrated Approach ◽  
Structure And Function ◽  
Dynamic Membrane ◽  
Biophysical Characterization ◽  
Intermediate States ◽  
And Function

Abstract ABC exporters are highly dynamic membrane proteins that span a huge spectrum of different conformations. A detailed integrated approach of cellular, biochemical and biophysical characterization of these ‘open’, ‘closed’ and other intermediate states is central to understanding their function. Almost 40 years after the discovery of the first ABC transporter, thanks to the enormous development in methodologies, a picture is slowly emerging to visualize how these fascinating molecules transport their substrates. This mini review summarizes some of the biophysical tools that have made a major impact in understanding the function of the ABC exporters.

Bacterial ß-Barrel Outer Membrane Proteins

2009 ◽  
pp. 182-207
Author(s):  
Pantelis G. Bagos ◽  
Stavros J. Hamodrakas
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Bacterial Cell ◽  
Outer Membrane Proteins ◽  
Structural Features ◽  
Structure And Function ◽  
Structural Motif ◽  
Functional Roles ◽  
Bacterial Outer Membrane ◽  
And Function

ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts. During the last few years, remarkable advances have been made towards an understanding of their functional and structural features. It is now wellknown that ß-barrels are performing a large variety of biologically important functions for the bacterial cell. Such functions include acting as specific or non-specific channels, receptors for various compounds, enzymes, translocation channels, structural proteins, and adhesion proteins. All these functional roles are of great importance for the survival of the bacterial cell under various environmental conditions or for the pathogenic properties expressed by these organisms. This chapter reviews the currently available literature regarding the structure and function of bacterial outer membrane proteins. We emphasize the functional diversity expressed by a common structural motif such as the ß-barrel, and we provide evidence from the current literature for dozens of newly discovered families of transmembrane ß-barrels.

Membrane proteins: is the future disc shaped?

2016 ◽  
Vol 44 (4) ◽  
pp. 1011-1018 ◽  
Author(s):  
Sarah C. Lee ◽  
Naomi L. Pollock
Keyword(s):  
Membrane Proteins ◽  
Maleic Acid ◽  
Membrane Lipids ◽  
Biological Membranes ◽  
Structure And Function ◽  
Amphiphilic Copolymer ◽  
New Approach ◽  
Analysis Techniques ◽  
Lipid Particles ◽  
And Function

The use of styrene maleic acid lipid particles (SMALPs) for the purification of membrane proteins (MPs) is a rapidly developing technology. The amphiphilic copolymer of styrene and maleic acid (SMA) disrupts biological membranes and can extract membrane proteins in nanodiscs of approximately 10 nm diameter. These discs contain SMA, protein and membrane lipids. There is evidence that MPs in SMALPs retain their native structures and functions, in some cases with enhanced thermal stability. In addition, the method is compatible with biological buffers and a wide variety of biophysical and structural analysis techniques. The use of SMALPs to solubilize and stabilize MPs offers a new approach in our attempts to understand, and influence, the structure and function of MPs and biological membranes. In this review, we critically assess progress with this method, address some of the associated technical challenges, and discuss opportunities for exploiting SMA and SMALPs to expand our understanding of MP biology.

Structure and Function of Membrane Proteins.

MEMBRANE ◽  
1996 ◽  
Vol 21 (4) ◽  
pp. 230-239
Author(s):  
Tetsuji Okada ◽  
Tsutomu Kouyama
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
And Function

scholarly journals Membrane proteins in nanotechnology

2013 ◽  
Vol 35 (1) ◽  
pp. 4-8
Author(s):  
Paul Curnow
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
High Performance ◽  
Natural World ◽  
Structure And Function ◽  
One Dimension ◽  
Modern Life ◽  
Protein Structure And Function ◽  
Exciting Current ◽  
And Function

The potential for nanotechnology to transform modern life has been appreciated for several years. Generally, nanotechnology involves objects with at least one dimension of less than 100 nm. Such stuff is abundant in the natural world, and one of the most exciting current areas in nanoscience research is the use of proteins as nanoscale components of high-performance devices and as nanosized tools in their own right. Biochemists, with our relatively sophisticated and mature toolkit for understanding protein structure and function, are now saddling up to explore the wild frontiers of biological nanotechnology.

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