BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 




Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


» Online Users: 51
0 members and 51 guests
No Members online
Most users ever online was 292, 07-25-2011 at 03:18 PM.
» Welcome!

Welcome, NMR world!


Our visitors map.


» Log in
User Name Not a member yet?
Register Now!
Password
Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix, MiTeGen etc. - Jewish Life News

Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix, MiTeGen etc. Jewish Life News Read here
0 Replies | 57 Views
(2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast - Cole of Duty
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar (2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast - Cole of Duty

(2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast Cole of Duty Read here
0 Replies | 79 Views
[NMR paper] Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.

Related Articles Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.

Prog Nucl Magn Reson Spectrosc. 2020 Apr;117:70-88

Authors: De Biasi F, Mancin F, Rastrelli F

Abstract
Sensing methodologies for the detection of target compounds in mixtures are important in many different contexts, ranging from medical diagnosis to environmental analysis and quality assessment. Ideally, such detection methods should allow for both identification and quantification of the targets, minimizing the possibility of false positives. With very few exceptions, most of the available sensing techniques rely on the selective interaction of the analyte with some detector, which in turn produces a signal as a result of the interaction. This approach hence provides indirect information on the targets, whose identity is generally ensured by comparison with known standards, if available, or by the selectivity of the sensor system itself. Pursuing a different approach, NMR chemosensing aims at generating signals directly from the analytes, in the form of a (complete) NMR spectrum. In this way, not only are the targets unequivocally identified, but it also becomes possible to identify and assign the structures of unknown species. In this review we show how relaxation- and diffusion-based NMR techniques, assisted by appropriate... [Read More]
0 Replies | 54 Views
[NMR paper] A solid-state NMR tool box for the investigation of ATP-fueled protein engines.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar A solid-state NMR tool box for the investigation of ATP-fueled protein engines.

Related Articles A solid-state NMR tool box for the investigation of ATP-fueled protein engines.

Prog Nucl Magn Reson Spectrosc. 2020 Apr;117:1-32

Authors: Wiegand T

Abstract
Motor proteins are involved in a variety of cellular processes. Their main purpose is to convert the chemical energy released during adenosine triphosphate (ATP) hydrolysis into mechanical work. In this review, solid-state Nuclear Magnetic Resonance (NMR) approaches are discussed allowing studies of structures, conformational events and dynamic features of motor proteins during a variety of enzymatic reactions. Solid-state NMR benefits from straightforward sample preparation based on sedimentation of the proteins directly into the Magic-Angle Spinning (MAS) rotor. Protein resonance assignment is the crucial and often time-limiting step in interpreting the wealth of information encoded in the NMR spectra. Herein, potentials, challenges and limitations in resonance assignment for large motor proteins are presented, focussing on both biochemical and spectroscopic approaches. This work highlights NMR tools available to study the action of the motor domain and its coupling to... [Read More]
0 Replies | 27 Views
[NMR paper] ShiftCrypt: a web server to understand and biophysically align proteins through their NMR chemical shift values.
May 29, 2020 - 4:59 PM - by nmrlearner
nmrlearner's Avatar ShiftCrypt: a web server to understand and biophysically align proteins through their NMR chemical shift values.

Related Articles ShiftCrypt: a web server to understand and biophysically align proteins through their NMR chemical shift values.

Nucleic Acids Res. 2020 May 27;:

Authors: Orlando G, Raimondi D, Kagami LP, Vranken WF

Abstract
Nuclear magnetic resonance (NMR) spectroscopy data provides valuable information on the behaviour of proteins in solution. The primary data to determine when studying proteins are the per-atom NMR chemical shifts, which reflect the local environment of atoms and provide insights into amino acid residue dynamics and conformation. Within an amino acid residue, chemical shifts present multi-dimensional and complexly cross-correlated information, making them difficult to analyse. The ShiftCrypt method, based on neural network auto-encoder architecture, compresses the per-amino acid chemical shift information in a single, interpretable, amino acid-type independent value that reflects the biophysical state of a residue. We here present the ShiftCrypt web server, which makes the method readily available. The server accepts... [Read More]
0 Replies | 45 Views
[NMR paper] A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.
May 29, 2020 - 4:59 PM - by nmrlearner
nmrlearner's Avatar A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.

Related Articles A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.

Proc Natl Acad Sci U S A. 2020 May 26;:

Authors: Abramov G, Velyvis A, Rennella E, Wong LE, Kay LE

Abstract
The development of methyl-transverse relaxation-optimized spectroscopy (methyl-TROSY)-based NMR methods, in concert with robust strategies for incorporation of methyl-group probes of structure and dynamics into the protein of interest, has facilitated quantitative studies of high-molecular-weight protein complexes. Here we develop a one-pot in vitro reaction for producing NMR quantities of methyl-labeled DNA at the C5 and N6 positions of cytosine (5mC) and adenine (6mA) nucleobases, respectively, enabling the study of high-molecular-weight DNA molecules using TROSY approaches originally developed for protein applications. Our biosynthetic strategy exploits the large number of naturally available methyltransferases to specifically methylate DNA at a desired number of sites that serve as probes of structure and dynamics. We illustrate the methodology with studies of the 153-base pair Widom DNA molecule that is simultaneously methyl-labeled at five sites, showing that high-quality 13C-1H spectra can be recorded on 100 ?M samples in a few minutes. NMR spin relaxation studies of labeled methyl groups in both DNA and... [Read More]
0 Replies | 42 Views
Prediction of flow effects in quantitative NMR measurements
May 29, 2020 - 4:59 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Prediction of flow effects in quantitative NMR measurements

Friebel, Anne, Thomas Specht, Erik von Harbou, Kerstin Münnemann, and Hans Hasse. “Prediction of Flow Effects in Quantitative NMR Measurements.” Journal of Magnetic Resonance 312 (March 2020): 106683.


https://doi.org/10.1016/j.jmr.2020.106683.


A method for the prediction of the magnetization in flow NMR experiments is presented, which can be applied to mixtures. It enables a quantitative evaluation of NMR spectra of flowing liquid samples even in cases in which the magnetization is limited by the flow. A transport model of the nuclei’s magnetization, which is based on the Bloch-equations, is introduced into a computational fluid dynamics (CFD) code. This code predicts the velocity field and relative magnetization of different nuclei for any chosen flow cell geometry, fluid and flow rate. The prediction of relative magnetization is used to correct the observed reduction of signal intensity caused by incomplete premagnetization in fast flowing liquids. By means of the model, quantitative NMR measurements at high flow rates are possible. The method is predictive and enables calculating correction factors for any flow cell design and operating condition based on simple static T1 time measurements. This makes time-consuming calibration measurements for assessing the influence of flow effects obsolete, which otherwise would have to be carried out for each studied condition. The new method is especially interesting for flow measurements with compact medium field NMR spectrometers, which have small premagnetization... [Read More]
0 Replies | 31 Views
[ssNMR] Post-doc position in the Nieuwkoop Lab
May 29, 2020 - 4:59 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[ssNMR] Post-doc position in the Nieuwkoop Lab



The Nieuwkoop lab seeks a post-doctoral researcher to help start a project on the structural biology of the PTEN protein. We use fast spinning solid-state NMR to study protein-lipid interactions. In this project, we seek to understand the functional role of PIP binding by the C2 domain of PTEN. The PTEN C2 domain will be expressed with isotopic labeling to for backbone and side-chain NMR assignments as nanocrystals and bound to its PIP ligand in liposomes. This project will depend on novel ssNMR experiments, optimized sample preparation, and specialized NMR equipment to assess structural and dynamical changes in the bound and unbound protein.


Contact Andy at an567@chem.rutgers.edu for more details and apply here: http://jobs.rutgers.edu/postings/101163


Go to The DNP-NMR Blog for more info.
0 Replies | 41 Views
» Stats
Members: 3,202
Threads: 22,731
Posts: 23,117
Top Poster: nmrlearner (20,175)
Welcome to our newest member, bpadmanabhan
Powered by vBadvanced CMPS v3.2.2

All times are GMT. The time now is 05:45 AM.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2020, Jelsoft Enterprises Ltd.
vBCredits II Deluxe v1.2.0 Copyright © 2010 DragonByte Technologies
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

Map