Transmembrane Domains in Membrane Protein Folding, Oligomerization, and Function

2008 ◽  
pp. 876-918 ◽  
Author(s):  
Anja Ridder ◽  
Dieter Langosch
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Transmembrane Domains ◽  
Membrane Protein Folding ◽  
And Function

scholarly journals Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport

2017 ◽  
Vol 372 (1726) ◽  
pp. 20160214 ◽  
Author(s):  
Nathan H. Joh ◽  
Gevorg Grigoryan ◽  
Yibing Wu ◽  
William F. DeGrado
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Protein Design ◽  
De Novo ◽  
Cell Signalling ◽  
Membrane Protein Folding ◽  
Cellular Processes ◽  
Membrane Pores ◽  
Self Assembling ◽  
And Function

Ion transporters and channels are able to identify and act on specific substrates among myriads of ions and molecules critical to cellular processes, such as homeostasis, cell signalling, nutrient influx and drug efflux. Recently, we designed Rocker, a minimalist model for Zn 2+ /H + co-transport. The success of this effort suggests that de novo membrane protein design has now come of age so as to serve a key approach towards probing the determinants of membrane protein folding, assembly and function. Here, we review general principles that can be used to design membrane proteins, with particular reference to helical assemblies with transport function. We also provide new functional and NMR data that probe the dynamic mechanism of conduction through Rocker. This article is part of the themed issue ‘Membrane pores: from structure and assembly, to medicine and technology’.

scholarly journals Local Bilayer Hydrophobicity Modulates Membrane Protein Stability

2020 ◽  
Author(s):  
Dagan C. Marx ◽  
Karen G. Fleming
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Hydrophobic Effect ◽  
Water Concentration ◽  
Side Chain ◽  
Interfacial Region ◽  
Side Chains ◽  
Free Energies ◽  
Membrane Protein Folding ◽  
And Function

ABSTRACTThrough the insertion of nonpolar side chains into the bilayer, the hydrophobic effect has long been accepted as a driving force for membrane protein folding. However, how the changing chemical composition of the bilayer affects the magnitude side chain transfer free energies has historically not been well understood. A particularly challenging region for experimental interrogation is the bilayer interfacial region that is characterized by a steep polarity gradient. In this study we have determined the for nonpolar side chains as a function of bilayer position using a combination of experiment and simulation. We discovered an empirical correlation between the surface area of nonpolar side chain, the transfer free energies, and the local water concentration in the membrane that allows for to be accurately estimated at any location in the bilayer. Using these water-to-bilayer values, we calculated the interface-to-bilayer transfer free energy . We find that the are similar to the “biological”, translocon-based transfer free energies, indicating that the translocon energetically mimics the bilayer interface. Together these findings can be applied to increase the accuracy of computational workflows used to identify and design membrane proteins, as well as bring greater insight into our understanding of how disease-causing mutations affect membrane protein folding and function.

scholarly journals Applications of Single-Molecule Methods to Membrane Protein Folding Studies

2018 ◽  
Vol 430 (4) ◽  
pp. 424-437 ◽  
Author(s):  
Robert E. Jefferson ◽  
Duyoung Min ◽  
Karolina Corin ◽  
Jing Yang Wang ◽  
James U. Bowie
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Single Molecule ◽  
Membrane Protein Folding

scholarly journals In-Situ Observation of Membrane Protein Folding during Cell-Free Expression

PLoS ONE ◽  
2016 ◽  
Vol 11 (3) ◽  
pp. e0151051 ◽  
Author(s):  
Axel Baumann ◽  
Silke Kerruth ◽  
Jörg Fitter ◽  
Georg Büldt ◽  
Joachim Heberle ◽  
...  
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Free Expression ◽  
In Situ Observation ◽  
Membrane Protein Folding

Membrane Protein Folding and Stability

2021 ◽  
pp. 137-160
Author(s):  
Stephen H. White ◽  
Gunnar von Heijne ◽  
Donald M. Engelman
Keyword(s):  
Protein Folding ◽  
Membrane Protein ◽  
Membrane Protein Folding
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