scholarly journals Tandem Facial Amphiphiles for Membrane Protein Stabilization

2010 ◽  
Vol 132 (47) ◽  
pp. 16750-16752 ◽  
Author(s):  
Pil Seok Chae ◽  
Kamil Gotfryd ◽  
Jennifer Pacyna ◽  
Larry J. W. Miercke ◽  
Søren G. F. Rasmussen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Stabilization

scholarly journals Membrane Protein Stabilization Strategies for Structural and Functional Studies

Membranes ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 155
Author(s):  
Ekaitz Errasti-Murugarren ◽  
Paola Bartoccioni ◽  
Manuel Palacín
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Membrane ◽  
Protein Stabilization ◽  
New Drugs ◽  
Cell Physiology ◽  
Protein Preparation ◽  
Functional Studies ◽  
Membrane Protein Stability ◽  
Druggable Targets

Accounting for nearly two-thirds of known druggable targets, membrane proteins are highly relevant for cell physiology and pharmacology. In this regard, the structural determination of pharmacologically relevant targets would facilitate the intelligent design of new drugs. The structural biology of membrane proteins is a field experiencing significant growth as a result of the development of new strategies for structure determination. However, membrane protein preparation for structural studies continues to be a limiting step in many cases due to the inherent instability of these molecules in non-native membrane environments. This review describes the approaches that have been developed to improve membrane protein stability. Membrane protein mutagenesis, detergent selection, lipid membrane mimics, antibodies, and ligands are described in this review as approaches to facilitate the production of purified and stable membrane proteins of interest for structural and functional studies.

scholarly journals Rationally Engineered Tandem Facial Amphiphiles for Improved Membrane Protein Stabilization Efficacy

ChemBioChem ◽  
2018 ◽  
Vol 19 (20) ◽  
pp. 2225-2232 ◽  
Author(s):  
Manabendra Das ◽  
Yang Du ◽  
Jonas S. Mortensen ◽  
Parameswaran Hariharan ◽  
Hyun Sung Lee ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Stabilization

scholarly journals Pendant-bearing glucose-neopentyl glycol (P-GNG) amphiphiles for membrane protein manipulation: Importance of detergent pendant chain for protein stabilization

2020 ◽  
Vol 112 ◽  
pp. 250-261
Author(s):  
Hyoung Eun Bae ◽  
Cristina Cecchetti ◽  
Yang Du ◽  
Satoshi Katsube ◽  
Jonas S. Mortensen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Stabilization ◽  
Neopentyl Glycol

scholarly journals Sparingly fluorinated maltoside-based surfactants for membrane-protein stabilization

2016 ◽  
Vol 40 (6) ◽  
pp. 5364-5378 ◽  
Author(s):  
Ange Polidori ◽  
Simon Raynal ◽  
Laurie-Anne Barret ◽  
Mohamed Dahani ◽  
Cherone Barrot-Ivolot ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Stabilization

A robust method to screen detergents for membrane protein stabilization, revisited

2016 ◽  
Vol 511 ◽  
pp. 31-35 ◽  
Author(s):  
Philippe Champeil ◽  
Stéphane Orlowski ◽  
Simon Babin ◽  
Sten Lund ◽  
Marc le Maire ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Stabilization ◽  
Robust Method

scholarly journals Intra-helical salt bridge contribution to membrane protein insertion

2021 ◽  
Author(s):  
Gerard Duart ◽  
John Lamb ◽  
Arne Elofsson ◽  
Ismael Mingarro
Keyword(s):  
Amino Acids ◽  
Membrane Protein ◽  
Electrostatic Interactions ◽  
Salt Bridge ◽  
Protein Stabilization ◽  
Membrane Insertion ◽  
Salt Bridges ◽  
Protein Insertion

ABSTRACTSalt bridges between negatively (D, E) and positively charged (K, R, H) amino acids play an important role in protein stabilization. This has a more prevalent effect in membrane proteins where polar amino acids are exposed to a very hydrophobic environment. In transmembrane (TM) helices the presence of charged residues can hinder the insertion of the helices into the membrane. This can sometimes be avoided by TM region rearrangements after insertion, but it is also possible that the formation of salt bridges could decrease the cost of membrane integration. However, the presence of intra-helical salt bridges in TM domains and their effect on insertion has not been properly studied yet. In this work, we use an analytical pipeline to study the prevalence of charged pairs of amino acid residues in TM α-helices, which shows that potentially salt-bridge forming pairs are statistically over-represented. We then selected some candidates to experimentally determine the contribution of these electrostatic interactions to the translocon-assisted membrane insertion process. Using both in vitro and in vivo systems, we confirm the presence of intra-helical salt bridges in TM segments during biogenesis and determined that they contribute between 0.5-0.7 kcal/mol to the apparent free energy of membrane insertion (ΔGapp). Our observations suggest that salt bridge interactions can be stabilized during translocon-mediated insertion and thus could be relevant to consider for the future development of membrane protein prediction software.

scholarly journals Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins

Crystals ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 1032
Author(s):  
Sonia Khemaissa ◽  
Sandrine Sagan ◽  
Astrid Walrant
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Hydrogen Bonds ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Noncovalent Interactions ◽  
Chemical Properties ◽  
Protein Stabilization ◽  
Physico Chemical

Tryptophan is an aromatic amino acid with unique physico-chemical properties. It is often encountered in membrane proteins, especially at the level of the water/bilayer interface. It plays a role in membrane protein stabilization, anchoring and orientation in lipid bilayers. It has a hydrophobic character but can also engage in many types of interactions, such as π–cation or hydrogen bonds. In this review, we give an overview of the role of tryptophan in membrane proteins and a more detailed description of the underlying noncovalent interactions it can engage in with membrane partners.

Membrane protein stability depends on the concentration of compatible solutes – a single molecule force spectroscopic study

2013 ◽  
Vol 394 (11) ◽  
pp. 1465-1474 ◽  
Author(s):  
Arpita Roychoudhury ◽  
Adeline Bieker ◽  
Dieter Häussinger ◽  
Filipp Oesterhelt
Keyword(s):  
Membrane Protein ◽  
Protein Stability ◽  
Single Molecule ◽  
Protein Unfolding ◽  
Compatible Solutes ◽  
Protein Stabilization ◽  
Intramolecular Interactions ◽  
Organic Osmolytes ◽  
Dynamic Relationship ◽  
The Impact

Abstract Compatible solutes are small, uncharged, zwitter ionic, osmotically active molecules produced and accumulated by microorganisms inside their cell to counteract different kinds of environmental stress. They enhance protein stability without interfering with the metabolic pathways even at molar concentrations. In this paper, we report the stabilizing effects of compatible solutes, ectoine, betaine and taurine on membrane protein bacteriorhodopsin at different concentrations. Using atomic force microscopy based single molecule force spectroscopy the impact of the osmolytes was quantified by measuring the forces required to pull the protein out of the membrane and the change in the persistence lengths of the unfolded polypeptide chain. Increase in unfolding forces were observed, indicating the strengthening of intramolecular interactions, which are vital for protein stability. The decrease in persistence lengths was recorded and showed increasing tendencies of the polypeptide strand to coil up. Interestingly, it was revealed that these molecules have different stabilizing effects on protein unfolding at different concentrations. The results show that the unfolding of single protein provides insight to the structure-dynamic relationship between the protein and compatible solute molecules at sub-nanometer scale. This also helps to understand the molecular mechanism involved in protein stabilization by organic osmolytes.

Trehalose-cored amphiphiles for membrane protein stabilization: importance of the detergent micelle size in GPCR stability

2019 ◽  
Vol 17 (12) ◽  
pp. 3249-3257 ◽  
Author(s):  
Manabendra Das ◽  
Yang Du ◽  
Jonas S. Mortensen ◽  
Manuel Ramos ◽  
Lubna Ghani ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Stabilization ◽  
Detergent Micelle ◽  
Micelle Size

A novel class of non-chromophoric trehalose-cored amphiphiles was developed and some of the detergents displayed favorable behavior in stabilizing membrane proteins.

scholarly journals A Comprehensive Computational Study of Amino Acid Interactions in Membrane Proteins

2019 ◽  
Author(s):  
Mame Ndew Mbaye ◽  
Qingzhen Hou ◽  
Sankar Basu ◽  
Fabian Teheux ◽  
Fabrizio Pucci ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Computational Study ◽  
Globular Proteins ◽  
Protein Stabilization ◽  
Energy Functions ◽  
Hydrophobic Residues ◽  
Polar Residues ◽  
Transmembrane Regions

AbstractTransmembrane proteins play a fundamental role in a wide series of biological processes but, despite their importance, they are less studied than globular proteins, essentially because their embedding in lipid membranes hampers their experimental characterization. In this paper, we improved our understanding of their structural stability through the development of new knowledge-based energy functions describing amino acid pair interactions that prevail in the transmembrane and extramembrane regions of membrane proteins. The comparison of these potentials and those derived from globular proteins yields an objective view of the relative strength of amino acid interactions in the different protein environments, and their role in protein stabilization. Separate potentials were also derived from α-helical and β-barrel transmembrane regions to investigate possible dissimilarities. We found that, in extramembrane regions, hydrophobic residues are less frequent but interactions between aromatic and aliphatic amino acids as well as aromatic-sulfur interactions contribute more to stability. In transmembrane regions, polar residues are less abundant but interactions between residues of equal or opposite charges or non-charged polar residues as well as anion-π interactions appear stronger. This shows indirectly the preference of the water and lipid molecules to interact with polar and hydrophobic residues, respectively. We applied these new energy functions to predict whether a residue is located in the trans- or extramembrane region, and obtained an AUC score of 83% in cross validation, which demonstrates their accuracy. As their application is, moreover, extremely fast, they are optimal instruments for membrane protein design and large-scale investigations of membrane protein stability.

Sign in / Sign up

Export Citation Format

Share Document