scholarly journals Thermostability Assays: a Generic and Versatile Tool for Studying the Functional and Structural Properties of Membrane Proteins in Detergents

2020 ◽  
pp. 105-121
Author(s):  
Steven P. D. Harborne ◽  
Martin S. King ◽  
Edmund R. S. Kunji
Keyword(s):  
Membrane Proteins ◽  
Structural Properties ◽  
Versatile Tool

scholarly journals Contrast-Matched Isotropic Bicelles: A Versatile Tool to Specifically Probe the Solution Structure of Peripheral Membrane Proteins Using SANS

Langmuir ◽  
2017 ◽  
Vol 33 (26) ◽  
pp. 6572-6580 ◽  
Author(s):  
Raphael Dos Santos Morais ◽  
Olivier Delalande ◽  
Javier Pérez ◽  
Liza Mouret ◽  
Arnaud Bondon ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Solution Structure ◽  
Peripheral Membrane Proteins ◽  
Versatile Tool

scholarly journals Recent innovations in membrane-protein structural biology

F1000Research ◽  
2019 ◽  
Vol 8 ◽  
pp. 211 ◽  
Author(s):  
James P Allen
Keyword(s):  
Membrane Proteins ◽  
Structural Properties ◽  
Protein Function ◽  
Three Dimensional ◽  
Protein Crystals ◽  
Experimental Investigations ◽  
X Ray Diffraction ◽  
Single Particles ◽  
X Ray ◽  
New Instrumentation

Innovations are expanding the capabilities of experimental investigations of the structural properties of membrane proteins. Traditionally, three-dimensional structures have been determined by measuring x-ray diffraction using protein crystals with a size of least 100 μm. For membrane proteins, achieving crystals suitable for these measurements has been a significant challenge. The availabilities of micro-focus x-ray beams and the new instrumentation of x-ray free-electron lasers have opened up the possibility of using submicrometer-sized crystals. In addition, advances in cryo-electron microscopy have expanded the use of this technique for studies of protein crystals as well as studies of individual proteins as single particles. Together, these approaches provide unprecedented opportunities for the exploration of structural properties of membrane proteins, including dynamical changes during protein function.

scholarly journals 3P-099 Prediction of residue-level structural properties of membrane proteins(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S142-S143
Author(s):  
Hemjit Singh ◽  
VK Krishna Mohan ◽  
Yogesh Paudel ◽  
Shandar Ahmad ◽  
Kenji Mizuguchi
Keyword(s):  
Membrane Proteins ◽  
Annual Meeting ◽  
Structural Properties ◽  
Residue Level ◽  
Biophysical Society

Solid-supported lipid bilayers – A versatile tool for the structural and functional characterization of membrane proteins

Methods ◽  
2020 ◽  
Vol 180 ◽  
pp. 56-68 ◽  
Author(s):  
Jakob Andersson ◽  
Pierluigi Bilotto ◽  
Laura L.E. Mears ◽  
Stefan Fossati ◽  
Ulrich Ramach ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Functional Characterization ◽  
Supported Lipid Bilayers ◽  
Versatile Tool

19F NMR as a versatile tool to study membrane protein structure and dynamics

2019 ◽  
Vol 400 (10) ◽  
pp. 1277-1288 ◽  
Author(s):  
Dania Rose-Sperling ◽  
Mai Anh Tran ◽  
Luca M. Lauth ◽  
Benedikt Goretzki ◽  
Ute A. Hellmich
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Membrane Protein Structure ◽  
X Ray Crystallography ◽  
Measurement Analysis ◽  
Functional Dynamics ◽  
Ligand Interactions ◽  
Versatile Tool ◽  
G Protein Coupled

AbstractTo elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as membrane transporters, ion channels or G-protein coupled receptors (GPCRs), the incorporation of a single reporter at a select site can significantly simplify the observables and the measurement/analysis requirements. Here we present examples using19F nuclear magnetic resonance (NMR) spectroscopy as a powerful, yet relatively straightforward tool to study (membrane) protein structure, dynamics and ligand interactions. We summarize methods to incorporate19F labels into proteins and discuss the type of information that can be readily obtained for membrane proteins already from relatively simple NMR spectra with a focus on GPCRs as the membrane protein family most extensively studied by this technique. In the future, these approaches may be of particular interest also for many proteins that undergo complex functional dynamics and/or contain unstructured regions and thus are not amenable to X-ray crystallography or cryo electron microscopy (cryoEM) studies.

scholarly journals α-Synuclein lipoprotein nanoparticles

2017 ◽  
Vol 6 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Cédric Eichmann ◽  
Stefan Bibow ◽  
Roland Riek
Keyword(s):  
Parkinson’S Disease ◽  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Lipid Vesicles ◽  
Present Review ◽  
Membrane Mimetic ◽  
Charged Membrane ◽  
Versatile Tool ◽  
Potential Use ◽  
28 Nm

AbstractApolipoprotein nanodiscs are a versatile tool in nanotechnology as membrane mimetics allowing, for example, the study of membrane proteins. It has recently been discovered that the Parkinson’s disease associated protein α-synuclein (α-Syn) can also form discoid-like lipoprotein nanoparticles. The present review highlights the observation that α-Syn has the properties to define stable and homogeneous populations of nanoparticles with diameters of 7–10 nm and 19–28 nm by modifying lipid vesicles or encapsulating lipid bilayers in a nanodisc-type fashion, respectively. In contrast to apolipoprotein nanodiscs, α-Syn nanoparticles can incorporate entirely negatively charged lipids emphasizing their potential use in nanotechnology as a negatively charged membrane mimetic.

scholarly journals 2P-078 Prediction of equilibrium and dynamic structural properties of membrane proteins(Membrane proteins,The 47th Annual Meeting of the Biophysical Society of Japan)

2009 ◽  
Vol 49 (supplement) ◽  
pp. S118
Author(s):  
Shandar Ahmad ◽  
Hemjit Singh ◽  
Yogesh Paudel ◽  
Takaharu Mori ◽  
Yuji Sugita ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Annual Meeting ◽  
Structural Properties ◽  
Biophysical Society

scholarly journals Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Ingrid Chamma ◽  
Mathieu Letellier ◽  
Corey Butler ◽  
Béatrice Tessier ◽  
Kok-Hong Lim ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Steric Hindrance ◽  
Transmembrane Protein ◽  
Super Resolution ◽  
Leucine Rich Repeat ◽  
Versatile Tool ◽  
Resolution Imaging ◽  
Dual Colour ◽  
Specific Labelling

Abstract The advent of super-resolution imaging (SRI) has created a need for optimized labelling strategies. We present a new method relying on fluorophore-conjugated monomeric streptavidin (mSA) to label membrane proteins carrying a short, enzymatically biotinylated tag, compatible with SRI techniques including uPAINT, STED and dSTORM. We demonstrate efficient and specific labelling of target proteins in confined intercellular and organotypic tissues, with reduced steric hindrance and no crosslinking compared with multivalent probes. We use mSA to decipher the dynamics and nanoscale organization of the synaptic adhesion molecules neurexin-1β, neuroligin-1 (Nlg1) and leucine-rich-repeat transmembrane protein 2 (LRRTM2) in a dual-colour configuration with GFP nanobody, and show that these proteins are diffusionally trapped at synapses where they form apposed trans-synaptic adhesive structures. Furthermore, Nlg1 is dynamic, disperse and sensitive to synaptic stimulation, whereas LRRTM2 is organized in compact and stable nanodomains. Thus, mSA is a versatile tool to image membrane proteins at high resolution in complex live environments, providing novel information about the nano-organization of biological structures.

Changes Occur in Plasma Membrane Turnover when K562 Leukemia Cells are Induced to Differentiate

1982 ◽  
Vol 40 ◽  
pp. 286-287
Author(s):  
L. M. Marshall
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Intracellular Transport ◽  
Parent Cell ◽  
Membrane Turnover ◽  
Coated Pits ◽  
Surface Distribution ◽  
Specific Proteins ◽  
Erythroleukemic Cell ◽  
Specific Membrane

A human erythroleukemic cell line, metabolically blocked in a late stage of erythropoiesis, becomes capable of differentiation along the normal pathway when grown in the presence of hemin. This process is characterized by hemoglobin synthesis followed by rearrangement of the plasma membrane proteins and culminates in asymmetrical cytokinesis in the absence of nuclear division. A reticulocyte-like cell buds from the nucleus-containing parent cell after erythrocyte specific membrane proteins have been sequestered into its membrane. In this process the parent cell faces two obstacles. First, to organize its erythrocyte specific proteins at one pole of the cell for inclusion in the reticulocyte; second, to reduce or abolish membrane protein turnover since hemoglobin is virtually the only protein being synthesized at this stage. A means of achieving redistribution and cessation of turnover could involve movement of membrane proteins by a directional lipid flow. Generation of a lipid flow towards one pole and accumulation of erythrocyte-specific membrane proteins could be achieved by clathrin coated pits which are implicated in membrane endocytosis, intracellular transport and turnover. In non-differentiating cells, membrane proteins are turned over and are random in surface distribution. If, however, the erythrocyte specific proteins in differentiating cells were excluded from endocytosing coated pits, not only would their turnover cease, but they would also tend to drift towards and collect at the site of endocytosis. This hypothesis requires that different protein species are endocytosed by the coated vesicles in non-differentiating than by differentiating cells.

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