scholarly journals 1P088 Study of Local Mobility of peripheral membrane protein PLC-δ1 by Solid State NMR(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S45
Author(s):  
Naoko Uekama ◽  
Satoru Tuzi ◽  
Hitoshi Yagisawa ◽  
Katsuyuki Nishimura
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Local Mobility ◽  
Peripheral Membrane Protein ◽  
Oral Presentations

How to Prepare Membrane Proteins for Solid-State NMR: A Case Study on the α-Helical Integral Membrane Protein Diacylglycerol Kinase from E. coli

ChemBioChem ◽  
2005 ◽  
Vol 6 (9) ◽  
pp. 1693-1700 ◽  
Author(s):  
Mark Lorch ◽  
Salem Faham ◽  
Christoph Kaiser ◽  
Ingrid Weber ◽  
A. James Mason ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein ◽  
E Coli

scholarly journals Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR

Biology ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 396
Author(s):  
Vivien Yeh ◽  
Alice Goode ◽  
Boyan B. Bonev
Keyword(s):  
Protein Structure ◽  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Basic Unit ◽  
Molecular Assemblies ◽  
Nmr Studies ◽  
Main Challenge

Biological membranes define the interface of life and its basic unit, the cell. Membrane proteins play key roles in membrane functions, yet their structure and mechanisms remain poorly understood. Breakthroughs in crystallography and electron microscopy have invigorated structural analysis while failing to characterise key functional interactions with lipids, small molecules and membrane modulators, as well as their conformational polymorphism and dynamics. NMR is uniquely suited to resolving atomic environments within complex molecular assemblies and reporting on membrane organisation, protein structure, lipid and polysaccharide composition, conformational variations and molecular interactions. The main challenge in membrane protein studies at the atomic level remains the need for a membrane environment to support their fold. NMR studies in membrane mimetics and membranes of increasing complexity offer close to native environments for structural and molecular studies of membrane proteins. Solution NMR inherits high resolution from small molecule analysis, providing insights from detergent solubilised proteins and small molecular assemblies. Solid-state NMR achieves high resolution in membrane samples through fast sample spinning or sample alignment. Recent developments in dynamic nuclear polarisation NMR allow signal enhancement by orders of magnitude opening new opportunities for expanding the applications of NMR to studies of native membranes and whole cells.

scholarly journals Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State

2021 ◽  
Vol 8 ◽  
Author(s):  
Reza Amani ◽  
Charles D. Schwieters ◽  
Collin G. Borcik ◽  
Isaac R. Eason ◽  
Ruixian Han ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Structural Quality ◽  
Nmr Structures ◽  
Kir Channel ◽  
C Terminus ◽  
Water Accessibility ◽  
Distance Restraints

NMR structures of membrane proteins are often hampered by poor chemical shift dispersion and internal dynamics which limit resolved distance restraints. However, the ordering and topology of these systems can be defined with site-specific water or lipid proximity. Membrane protein water accessibility surface area is often investigated as a topological function via solid-state NMR. Here we leverage water-edited solid-state NMR measurements in simulated annealing calculations to refine a membrane protein structure. This is demonstrated on the inward rectifier K+ channel KirBac1.1 found in Burkholderia pseudomallei. KirBac1.1 is homologous to human Kir channels, sharing a nearly identical fold. Like many existing Kir channel crystal structures, the 1p7b crystal structure is incomplete, missing 85 out of 333 residues, including the N-terminus and C-terminus. We measure solid-state NMR water proximity information and use this for refinement of KirBac1.1 using the Xplor-NIH structure determination program. Along with predicted dihedral angles and sparse intra- and inter-subunit distances, we refined the residues 1–300 to atomic resolution. All structural quality metrics indicate these restraints are a powerful way forward to solve high quality structures of membrane proteins using NMR.

Solid state NMR of membrane proteins: methods and applications

2021 ◽  
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Lipid Membrane ◽  
Cell Function ◽  
Membrane Lipid ◽  
Pharmacological Intervention ◽  
Nmr Methods ◽  
Informative Approach

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

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