Related ArticlesThe power, pitfalls and potential of the nanodisc system for NMR-based studies.
Biol Chem. 2016 Jul 23;
Authors: Viegas A, Viennet T, Etzkorn M
Abstract
The choice of a suitable membrane mimicking environment is of fundamental importance for the characterization of structure and function of membrane proteins. In this respect, usage of the lipid bilayer nanodisc technology provides a unique potential for NMR-based studies. This review summarizes the recent advances in this field, focusing on (i) the strengths of the system, (ii) the bottlenecks that may be faced as well as (iii) promising capabilities that may be explored in future studies.
PMID: 27451995 [PubMed - as supplied by publisher]
[NMR paper] MAS solid state NMR of proteins: simultaneous (15)N- (13)CA and (15)N- (13)CO dipolar recoupling via low-power symmetry-based RF pulse schemes.
MAS solid state NMR of proteins: simultaneous (15)N- (13)CA and (15)N- (13)CO dipolar recoupling via low-power symmetry-based RF pulse schemes.
MAS solid state NMR of proteins: simultaneous (15)N- (13)CA and (15)N- (13)CO dipolar recoupling via low-power symmetry-based RF pulse schemes.
J Biomol NMR. 2015 Feb 25;
Authors: Herbst C, Bellstedt P, Görlach M, Ramachandran R
Abstract
The generation of efficient RN n (?)s,(?)k symmetry-based low-power RF pulse schemes for simultaneous (15)N-(13)CA and (15)N-(13)CO dipolar recoupling...
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02-26-2015 11:11 PM
MAS solid state NMR of proteins: simultaneous 15 Nâ?? 13 CA and 15 Nâ?? 13 CO dipolar recoupling via low-power symmetry-based RF pulse schemes
MAS solid state NMR of proteins: simultaneous 15 Nâ?? 13 CA and 15 Nâ?? 13 CO dipolar recoupling via low-power symmetry-based RF pulse schemes
Abstract
The generation of efficient RN n νs,νk symmetry-based low-power RF pulse schemes for simultaneous 15Nâ??13CA and 15Nâ??13CO dipolar recoupling is demonstrated. The method involves mixing schemes employing phase and amplitude-modulated dual band-selective 180° pulses as basic â??Râ?? element and tailoring of the RF field-modulation...
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02-25-2015 05:56 PM
[NMR paper] Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Related Articles Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Chembiochem. 2014 Nov 18;
Authors: Rauthu SR, Shiao TC, André S, Miller MC, Madej E, Mayo KH, Gabius HJ, Roy R
Abstract
The emerging significance of...
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11-20-2014 08:40 PM
On the Potential of Hyperpolarized Water in Biomolecular NMR Studies
From The DNP-NMR Blog:
On the Potential of Hyperpolarized Water in Biomolecular NMR Studies
Harris, T., O. Szekely, and L. Frydman, On the Potential of Hyperpolarized Water in Biomolecular NMR Studies. The Journal of Physical Chemistry B, 2014. 118(12): p. 3281-3290.
http://dx.doi.org/10.1021/jp4102916
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07-07-2014 11:50 PM
[NMR paper] Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs
Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Beat Vögeli , Julien Orts , Dean Strotz , Celestine Chi , Martina Minges , Marielle Aulikki Wälti , Peter Güntert , Roland Riek</br>
Confined by the Boltzmann distribution of the energies of the states, a multitude of structural states are inherent to biomolecules. For a detailed understanding of a protein’s function, its entire...
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03-22-2014 01:28 AM
[NMR paper] Detergent/Nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.
Detergent/Nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Detergent/Nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.
PLoS One. 2013;8(1):e54378
Authors: Tzitzilonis C, Eichmann C, Maslennikov I, Choe...
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02-03-2013 10:19 AM
The Dynamics of Dendrimers by NMR Relaxation: Interpretation Pitfalls
The Dynamics of Dendrimers by NMR Relaxation: Interpretation Pitfalls
Luiz F. Pinto, Juan Correa, Manuel Martin-Pastor, Ricardo Riguera and Eduardo Fernandez-Megia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja311908n/aop/images/medium/ja-2012-11908n_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja311908n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/jMsa8SYap7o
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01-23-2013 09:47 AM
Chemical shift correlation at high MAS frequencies employing low-power symmetry-based mixing schemes
Chemical shift correlation at high MAS frequencies employing low-power symmetry-based mixing schemes
Abstract An approach for conveniently implementing low-power CN n ν and RN n ν symmetry-based band-selective mixing sequences for generating homo- and heteronuclear chemical shift correlation NMR spectra of low γ nuclei in biological solids is demonstrated. Efficient magnetisation transfer characteristics are achieved by selecting appropriate symmetries requiring the application of basic RF elements of relatively long duration and numerically tailoring the RF field modulation profile...