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: 195
0 members and 195 guests
No Members online
Most users ever online was 1,278, 01-09-2024 at 07:38 AM.
» Welcome!

Welcome, NMR world!


Our visitors map.


» Log in
User Name Not a member yet?
Register Now!
Password
[NMR paper] XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
Feb 27, 2024 - 9:30 PM - by nmrlearner
nmrlearner's Avatar XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures

The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO(2) and...

More...
0 Replies | 197 Views
Protein structure determination... blindfolded - Nature.com
Feb 27, 2024 - 9:20 AM - by nmrlearner
nmrlearner's Avatar Protein structure determination... blindfolded - Nature.com

Protein structure determination... blindfolded Nature.com Read here
0 Replies | 69 Views
Fluorine labelling for in situ 19F NMR in oriented systems
Feb 26, 2024 - 9:15 PM - by nmrlearner
nmrlearner's Avatar Fluorine labelling for in situ 19F NMR in oriented systems

Abstract

The focus of this project is to take advantage of the large NMR chemical shift anisotropy of 19F to determine the orientation of fluorine labeled biomolecules in situ in oriented biological systems such as muscle. The difficulty with a single fluorine atom is that the orientation determined from a chemical shift is not singlevalued in the case of a fully anisotropic chemical shift tensor. The utility of a labeling approach with two fluorine labels in a fixed molecular framework where one of the labels has an axially symmetric chemical shift anisotropy such as a CF3 group and the other has a fully asymmetric chemical shift anisotropy such as 5-fluorotryptophan is evaluated. The result is that the orientation of the label can be determined straightforwardly from a single one-dimensional 19F NMR spectrum. The potential applications are widespread and not limited to biological applications.



Source: Journal of Biomolecular NMR
0 Replies | 97 Views
A comprehensive assessment of selective amino acid 15N-labeling in human embryonic kidney 293 cells for NMR spectroscopy
Feb 26, 2024 - 9:15 PM - by nmrlearner
nmrlearner's Avatar A comprehensive assessment of selective amino acid 15N-labeling in human embryonic kidney 293 cells for NMR spectroscopy

Abstract

A large proportion of human proteins contain post-translational modifications that cannot be synthesized by prokaryotes. Thus, mammalian expression systems are often employed to characterize structure/function relationships using NMR spectroscopy. Here we define the selective isotope labeling of secreted, post-translationally modified proteins using human embryonic kidney (HEK)293 cells. We determined that alpha-[15N]- atoms from 10 amino acids experience minimal metabolic scrambling (C, F, H, K, M, N, R, T, W, Y). Two more interconvert to each other (G, S). Six others experience significant scrambling (A, D, E, I, L, V). We also demonstrate that tuning culture conditions suppressed V and I scrambling. These results define expectations for 15N-labeling in HEK293 cells.



Source: Journal of Biomolecular NMR
0 Replies | 54 Views
[NMR paper] A comprehensive assessment of selective amino acid (15)N-labeling in human embryonic kidney 293 cells for NMR spectroscopy
Feb 26, 2024 - 9:15 PM - by nmrlearner
nmrlearner's Avatar A comprehensive assessment of selective amino acid (15)N-labeling in human embryonic kidney 293 cells for NMR spectroscopy

A large proportion of human proteins contain post-translational modifications that cannot be synthesized by prokaryotes. Thus, mammalian expression systems are often employed to characterize structure/function relationships using NMR spectroscopy. Here we define the selective isotope labeling of secreted, post-translationally modified proteins using human embryonic kidney (HEK)293 cells. We determined that alpha-[^(15)N]- atoms from 10 amino acids experience minimal metabolic scrambling (C, F,...

More...
0 Replies | 55 Views
[NMR paper] Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR
Feb 26, 2024 - 9:15 PM - by nmrlearner
nmrlearner's Avatar Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR

With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies.

More...
0 Replies | 61 Views
[NMR paper] Protein-Cadmium Interactions in Crowded Biomolecular Environments Probed by In-cell and Lysate NMR Spectroscopy
Feb 26, 2024 - 9:15 PM - by nmrlearner
nmrlearner's Avatar Protein-Cadmium Interactions in Crowded Biomolecular Environments Probed by In-cell and Lysate NMR Spectroscopy

One of the mechanisms by which toxic metal ions interfere with cellular functions is ionic mimicry, where they bind to protein sites in lieu of native metals Ca ^(2+) and Zn ^(2+) . The influence of crowded intracellular environments on these interactions is not well understood. Here, we demonstrate the application of in-cell and lysate NMR spectroscopy to obtain atomic-level information on how a potent environmental toxin cadmium interacts with its protein targets. The experiments, conducted in...

More...
0 Replies | 68 Views
» Stats
Members: 3,202
Threads: 25,691
Posts: 26,077
Top Poster: nmrlearner (23,135)
Welcome to our newest member, bpadmanabhan
Powered by vBadvanced CMPS v3.2.2

All times are GMT. The time now is 05:16 AM.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, 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