scholarly journals An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins

2017 ◽  
Vol 139 (42) ◽  
pp. 14829-14832 ◽  
Author(s):  
Chih-Ta Henry Chien ◽  
Lukas R. Helfinger ◽  
Mark J. Bostock ◽  
Andras Solt ◽  
Yi Lei Tan ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Phospholipid Membrane ◽  
Nmr Studies ◽  
Membrane Mimetic

Membrane mimetics for solution NMR studies of membrane proteins

2017 ◽  
Vol 6 (1) ◽  
pp. 15-32 ◽  
Author(s):  
Konstantin S. Mineev ◽  
Kirill D. Nadezhdin
Keyword(s):  
Membrane Proteins ◽  
Structural Biology ◽  
Bilayer Membrane ◽  
Solution Nmr ◽  
Nmr Studies ◽  
Membrane Mimetic ◽  
Solution Nmr Spectroscopy ◽  
Solution Nuclear Magnetic Resonance ◽  
Specific Membrane ◽  
Selection Of

AbstractMembrane proteins are one of the most challenging and attractive objects in modern structural biology, as they are targets for the majority of medicines. However, studies of membrane proteins are hindered by several obstacles, including their low ability to crystallize, highly dynamic behavior of some of their domains, and need for membrane-like environment. Although solution nuclear magnetic resonance (NMR) is a very powerful technique of structural biology in terms of the amount of provided data, it imposes several limitations on the object under investigation, with the main constraint being related to the size of the object. For this reason, the membrane mimetic has to form particles of small size and simultaneously to properly simulate the bilayer membrane to be applicable for solution NMR spectroscopy. Here we review the recent advances in the field of membrane mimetics for solution NMR studies, discuss the advantages and drawbacks of specific membrane-like environments, and formulate the criteria for the selection of proper environment for a particular membrane protein or domain.

Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments

2019 ◽  
pp. 143-185 ◽  
Author(s):  
Erik Henrich ◽  
Frank Löhr ◽  
Julija Mezhyrova ◽  
Aisha Laguerre ◽  
Frank Bernhard ◽  
...  
Keyword(s):  
Synthetic Biology ◽  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media

2014 ◽  
Vol 247 (9-10) ◽  
pp. 827-842 ◽  
Author(s):  
Noelya Planchard ◽  
Élodie Point ◽  
Tassadite Dahmane ◽  
Fabrice Giusti ◽  
Marie Renault ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

Solution NMR studies of polytopic α-helical membrane proteins

2011 ◽  
Vol 21 (4) ◽  
pp. 497-508 ◽  
Author(s):  
Daniel Nietlispach ◽  
Antoine Gautier
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

scholarly journals ANTH domains within CALM, HIP1R, and Sla2 recognize ubiquitin internalization signals.

2021 ◽  
Author(s):  
Natalya Pashkova ◽  
Lokesh Gakhar ◽  
Stanley Winistorfer ◽  
Annabel Y Minard ◽  
Nicholas J Schnicker ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Proteins ◽  
Binding Proteins ◽  
Terminal Region ◽  
Regulatory Mechanisms ◽  
Solution Nmr ◽  
Nmr Studies ◽  
Binding Domains ◽  
Binding Regions

Ubiquitin (Ub) serves as a signal for clathrin-mediated endocytosis (CME) by engaging Ub-binding proteins with the internalization apparatus. Ub is a versatile internalization signal because it can be added to a wide variety of membrane proteins, expanding the capacity of cells to use a variety of regulatory mechanisms to specify the conditions under which a particular protein will be internalized. Several candidate adaptors that can recognize ubiquitinated membrane proteins have been identified that work in endocytic processes that are both clathrin-dependent and independent. These include Epsin and Eps15, which bind and help sort Ub-cargo into internalization sites. Here we identify additional components of the endocytosis apparatus that bind Ub. The N-terminal ANTH domains found in CALM, AP180, HIP1R and yeast Sla2 all bind monoubiquitin with micromolar affinity. ANTH domains belong to a larger superfamily of domains including ENTH and VHS domains, many of which have Ub-binding regions outside of their VHS/ENTH/ANTH domains that enable them to mediate Ub-dependent sorting events throughout the cell. Solution NMR studies combined with a crystal structure of the CALM ANTH domain in a complex with Ub show that Ub binds to a C-terminal region of the ANTH domain that is not present in ENTH domains. Combined loss of Ub-binding by ANTH-domain proteins and other Ub-binding domains within the internalization apparatus of yeast caused defects in the Ub-dependent internalization of the GPCR Ste2 but had no effect on internalization of Ste2 via other internalization signals. These studies define new components of the internalization machinery that work collectively with Epsin and Eps15 to specify recognition of Ub as an internalization signal.

scholarly journals Solution NMR studies of the integral membrane proteins OmpX and OmpA fromEscherichia coli

FEBS Letters ◽  
2001 ◽  
Vol 504 (3) ◽  
pp. 173-178 ◽  
Author(s):  
César Fernández ◽  
Christian Hilty ◽  
Sophie Bonjour ◽  
Koba Adeishvili ◽  
Konstantin Pervushin ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies ◽  
Fromescherichia Coli

Membrane mimetics for solution NMR studies of membrane proteins

nano Online ◽  
2018 ◽  
Author(s):  
Konstantin S. Mineev ◽  
Kirill D. Nadezhdin
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

scholarly journals Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins

2015 ◽  
Vol 61 (3-4) ◽  
pp. 261-274 ◽  
Author(s):  
Iga Kucharska ◽  
Thomas C. Edrington ◽  
Binyong Liang ◽  
Lukas K. Tamm
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies
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