Long-Term-Stable Ether−Lipid vs Conventional Ester−Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides

2011 ◽  
Vol 115 (8) ◽  
pp. 1767-1774 ◽  
Author(s):  
Kresten Bertelsen ◽  
Brian Vad ◽  
Erik H. Nielsen ◽  
Sara K. Hansen ◽  
Troels Skrydstrup ◽  
...  
Keyword(s):  
Solid State ◽  
Antimicrobial Peptides ◽  
Solid State Nmr ◽  
Structural Information ◽  
Ether Lipid

Protein structure by solid-state NMR spectroscopy

1987 ◽  
Vol 19 (1-2) ◽  
pp. 7-49 ◽  
Author(s):  
S. J. Opella ◽  
P. L. Stewart ◽  
K. G. Valentine
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Information ◽  
Biological Systems ◽  
Genetic Regulation ◽  
Protein Structures ◽  
Crystalline Solid ◽  
Solid State Nmr Spectroscopy ◽  
Nmr Methods

The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

scholarly journals Higher Magnetic Fields, Finer MOF Structural Information: 17O Solid-State NMR at 35.2 T

2020 ◽  
Vol 142 (35) ◽  
pp. 14877-14889 ◽  
Author(s):  
Vinicius Martins ◽  
Jun Xu ◽  
Xiaoling Wang ◽  
Kuizhi Chen ◽  
Ivan Hung ◽  
...  
Keyword(s):  
Solid State ◽  
Magnetic Fields ◽  
Solid State Nmr ◽  
Structural Information

scholarly journals Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR

2020 ◽  
Vol 7 ◽  
Author(s):  
Thomas Wiegand ◽  
Denis Lacabanne ◽  
Anahit Torosyan ◽  
Julien Boudet ◽  
Riccardo Cadalbert ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr

scholarly journals Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II

2011 ◽  
Vol 101 (5) ◽  
pp. 1193-1201 ◽  
Author(s):  
Tae-Joon Park ◽  
Ji-Sun Kim ◽  
Hee-Chul Ahn ◽  
Yongae Kim
Keyword(s):  
Solid State ◽  
Antimicrobial Peptides ◽  
Solid State Nmr ◽  
Structural Studies

Structure of an aluminophosphate EMM-8: a multi-technique approach

2007 ◽  
Vol 63 (1) ◽  
pp. 56-62 ◽  
Author(s):  
Guang Cao ◽  
Mobae Afeworki ◽  
Gordon J. Kennedy ◽  
Karl G. Strohmaier ◽  
Douglas L. Dorset
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Solid State Nmr ◽  
Structural Information ◽  
Local Symmetry ◽  
Unit Cell ◽  
Local Environments ◽  
Synchrotron Powder Diffraction ◽  
The Relationship

The crystal structure of an aluminophosphate, EMM-8 (ExxonMobil Material #8), was determined in its calcined, anhydrous form from synchrotron powder diffraction data using the computer program FOCUS. A linkage of double four-ring (D4R) building units forms a two-dimensional framework with 12-MR and 8-MR channels, and differs from a similar SAPO-40 (AFR) framework only by the relationship between paired D4R units. Rietveld refinement reveals a fit of the model to the observed synchrotron data by R wp = 0.1118, R(F 2) = 0.1769. Local environments of the tetrahedral phosphorus and aluminium sites were established by solid-state NMR, which detects distinct differences between as-synthesized and calcined materials. Distinct, reversible changes in the local symmetry of the P and Al atoms were observed by NMR upon calcination and subsequent hydration. These NMR data provided important constraints on the number of tetrahedral (T) atoms per unit cell and the connectivities of the T atoms. Detailed local structural information obtained by solid-state NMR thereby guided the ultimate determination of the structure of AlPO EMM-8 from the powder data. Comparisons are made to the recently published crystal structure of the fluoride-containing, as-synthesized SSZ-51, indicating that the unit-cell symmetry, axial dimensions and framework structure are preserved after calcination.

scholarly journals Multiscale structure-properties analysis of photoactive nanocomposite materials

2014 ◽  
Vol 70 (a1) ◽  
pp. C739-C739
Author(s):  
EL-Eulmi Bendeif ◽  
Kuan-Ying Hsieh ◽  
Dominik Schaniel ◽  
Axel Gansmuller ◽  
Sébastien Pillet ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Changes ◽  
Structural Information ◽  
Multiscale Approach ◽  
Structural Characterisation ◽  
Atomic Pair Distribution Function ◽  
Guest Species ◽  
Potential Applications ◽  
Relationship Of

In the last decades, the confinement of various types of functional material in mesoporous silica matrices has been used to design hybrid organic-inorganic nanocomposites with unique and fascinating properties. Such nanocomposites have attracted considerable interest owing to their potential applications in various domains [1-2], while reports with precise structural information of such molecular nanomaterials are still rather scarce and quite disparate. However, in order to be able to derive a structure-functionality relationship of such hybrid complexes, a detailed description of the structural organisation of the guest species and of their immediate surrounding is absolutely mandatory. We show in this contribution that detailed structural information can be obtained by using an appropriate multiscale approach combining various experimental techniques such as X-ray total scattering coupled to atomic pair distribution function (PDF) and solid-state NMR spectroscopy. This multiscale approach does provide more extensive and accurate structural information [3]. The PDF approach has allowed the identification of the nature of the incorporated species and their arrangement as well as the distinction of the various existing phases: isolated molecules and nanoparticles. The multi-nuclei Solid State NMR investigation has provided information on both the amorphous host and the molecular guest and adds a dynamic dimension to the classical static structural characterisation. We also discuss the influence of the structural changes on the physical properties of the investigated materials

scholarly journals Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy

2021 ◽  
Vol 8 ◽  
Author(s):  
Patrick C. A. van der Wel
Keyword(s):  
Solid State ◽  
Structure Determination ◽  
Solid State Nmr ◽  
Structural Information ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Distance Measurements ◽  
Challenges And Opportunities ◽  
Molecule Interactions ◽  
Angle Spinning

In structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic distance measurements. In the current review, we examine the utility of ssNMR measurements of angular constraints, as a complement to distance-based structure determination. The focus is on direct measurements of angular restraints via the judicious recoupling of multiple anisotropic ssNMR parameters, such as dipolar couplings and chemical shift anisotropies. Recent applications are highlighted, with a focus on studies of nanocrystalline polypeptides, aggregated peptides and proteins, receptor-substrate interactions, and small molecule interactions with amyloid protein fibrils. The review also examines considerations of when and where ssNMR torsion angle experiments are (most) effective, and discusses challenges and opportunities for future applications.

scholarly journals Deuterium Solid State NMR Studies of Intact Bacteria Treated With Antimicrobial Peptides

2021 ◽  
Vol 2 ◽  
Author(s):  
Valerie Booth
Keyword(s):  
Solid State ◽  
Antimicrobial Peptides ◽  
Solid State Nmr ◽  
Model Membranes ◽  
Nmr Studies ◽  
Intact Cells ◽  
Whole Cells ◽  
H Nmr ◽  
Structure And Dynamics ◽  
Lipid Mixtures

Solid state NMR has been tremendously useful in characterizing the structure and dynamics of model membranes composed of simple lipid mixtures. Model lipid studies employing solid state NMR have included important work revealing how membrane bilayer structure and dynamics are affected by molecules such as antimicrobial peptides (AMPs). However, solid state NMR need not be applied only to model membranes, but can also be used with living, intact cells. NMR of whole cells holds promise for helping resolve some unsolved mysteries about how bacteria interact with AMPs. This mini-review will focus on recent studies using 2H NMR to study how treatment with AMPs affect membranes in intact bacteria.

scholarly journals Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by 2 H solid-state NMR

2016 ◽  
Vol 1858 (12) ◽  
pp. 2959-2964 ◽  
Author(s):  
Marwa Laadhari ◽  
Alexandre A. Arnold ◽  
Andrée E. Gravel ◽  
Frances Separovic ◽  
Isabelle Marcotte
Keyword(s):  
Solid State ◽  
Antimicrobial Peptides ◽  
Solid State Nmr ◽  
Aurein 1.2
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