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

Home Forums Wiki NMR feeds Downloads Register Today's Posts



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


» Online Users: 159
0 members and 159 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] Hydrogen bonding in duplex DNA probed by DNP enhanced solid-state NMR N-H bond length measurements
Dec 20, 2023 - 6:59 AM - by nmrlearner
nmrlearner's Avatar Hydrogen bonding in duplex DNA probed by DNP enhanced solid-state NMR N-H bond length measurements

Numerous biological processes and mechanisms depend on details of base pairing and hydrogen bonding in DNA. Hydrogen bonds are challenging to quantify by X-ray crystallography and cryo-EM due to difficulty of visualizing hydrogen atom locations but can be probed with site specificity by NMR spectroscopy in solution and the solid state with the latter particularly suited to large, slowly tumbling DNA complexes. Recently, we showed that low-temperature dynamic nuclear polarization (DNP) enhanced...

More...
0 Replies | 203 Views
Short and long range 2D 15Nâ??15N NMR correlations among peptide groups by novel solid state dipolar mixing schemes
Dec 19, 2023 - 11:26 AM - by nmrlearner
nmrlearner's Avatar Short and long range 2D 15Nâ??15N NMR correlations among peptide groups by novel solid state dipolar mixing schemes

Abstract

A recently developed homonuclear dipolar recoupling scheme, Adiabatic Linearly FREquency Swept reCOupling (AL FRESCO), was applied to record two-dimensional (2D) 15Nâ??15N correlations on uniformly 15N-labeled GB1 powders. A major feature exploited in these 15Nâ??15N correlations was AL FRESCOâ??s remarkably low RF power demands, which enabled seconds-long mixing schemes when establishing direct correlations. These 15Nâ??15N mixing schemes proved efficient regardless of the magic-angle spinning (MAS) rate and, being nearly free from dipolar truncation effects, they enabled the detection of long-range, weak dipolar couplings, even in the presence of strong short-range dipolar couplings. This led to a connectivity information that was significantly better than that obtained with spontaneously proton-driven, 15N spin-diffusion experiments. An indirect approach producing long-range 15Nâ??15N correlations was also tested, relying on short (ms-long) 1HNâ??1HN mixings schemes while applying AL FRESCO chirped pulses along the 15N channel. These indirect mixing schemes produced numerous long-distance Niâ??Ni±n (nâ??=â??2â??â??â??5) correlations, that might be useful for characterizing three-dimensional arrangements in proteins. Once again, these AL FRESCO mediated experiments proved more informative than variants based on spin-diffusion-based 1HNâ??1HN counterparts.



... [Read More]
0 Replies | 171 Views
[NMR paper] Short and long range 2D 15N-15N NMR correlations among peptide groups by novel solid state dipolar mixing schemes
Dec 19, 2023 - 11:26 AM - by nmrlearner
nmrlearner's Avatar Short and long range 2D 15N-15N NMR correlations among peptide groups by novel solid state dipolar mixing schemes

A recently developed homonuclear dipolar recoupling scheme, Adiabatic Linearly FREquency Swept reCOupling (AL FRESCO), was applied to record two-dimensional (2D) ^(15)N-^(15)N correlations on uniformly ^(15)N-labeled GB1 powders. A major feature exploited in these ^(15)N-^(15)N correlations was AL FRESCO's remarkably low RF power demands, which enabled seconds-long mixing schemes when establishing direct correlations. These ^(15)N-^(15)N mixing schemes proved efficient regardless of the...

More...
0 Replies | 112 Views
[NMR paper] Peptoid-based macrodiscs of variable lipid composition for structural studies of membrane proteins by oriented-sample solid-state NMR
Dec 15, 2023 - 5:49 AM - by nmrlearner
nmrlearner's Avatar Peptoid-based macrodiscs of variable lipid composition for structural studies of membrane proteins by oriented-sample solid-state NMR

Solid-state Nuclear Magnetic Resonance (NMR) in combination with magnetically aligned discoidal lipid mimics allows for studying the conformations of membrane proteins in planar, lipid-rich bilayer environments and at the physiological temperature. We have recently demonstrated the general applicability of macrodiscs composed of DMPC lipids and peptoid belts, which yield magnetic alignment and NMR spectroscopic resolution comparable or superior to detergent-containing bicelles. Here we report on...

More...
0 Replies | 389 Views
[NMR paper] Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure
Dec 15, 2023 - 5:49 AM - by nmrlearner
nmrlearner's Avatar Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure

It is increasingly recognized that very small proteins (?-proteins) are ubiquitously found in all species of the three domains of life, and that they fulfill important functions. The halophilic archaeon Haloferax volcanii contains 282 ?-proteins of less than 70 amino acids. Notably, 43 of these contain two C(P)XCG motifs, suggesting their potential to complex a zinc ion. To explore the significance of these proteins, 16 genes encoding C(P)XCG proteins had been deleted, and the majority of...

More...
0 Replies | 106 Views
[NMR paper] Richer than previously probed: An application of 1H NMR reveals one hundred metabolites using only fifty microliter serum
Dec 14, 2023 - 10:45 AM - by nmrlearner
nmrlearner's Avatar Richer than previously probed: An application of 1H NMR reveals one hundred metabolites using only fifty microliter serum

The classical approach restricts the detection of metabolites in serum samples by using nuclear magnetic resonance (NMR) spectroscopy; however, the presence of copious proteins and lipoproteins emphasize and necessitate the development of a contemporary, high-throughput tactic. To eliminate the lipoproteins and proteins from sera to engender filtered sera (FS), the study was executed with 50 ?l serum obtained from five healthy individuals with 5 years of age difference from 25 to 45 years old...

More...
0 Replies | 179 Views
[NMR paper] Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz
Dec 14, 2023 - 10:45 AM - by nmrlearner
nmrlearner's Avatar Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for characterizing biomolecules such as proteins and nucleic acids at atomic resolution. Increased magnetic field strengths drive progress in biomolecular NMR applications, leading to improved performance, e.g., higher resolution. A new class of NMR spectrometers with a 28.2 T magnetic field (1.2 GHz ¹H frequency) has been commercially available since the end of 2019. The availability of ultra-high-field NMR instrumentation...

More...
0 Replies | 98 Views
[NMR paper] Enlarging the scenario of site directed 19F labeling for NMR spectroscopy of biomolecules
Dec 14, 2023 - 10:45 AM - by nmrlearner
nmrlearner's Avatar Enlarging the scenario of site directed 19F labeling for NMR spectroscopy of biomolecules

The possibility of using selectively incorporated ^(19)F nuclei for NMR spectroscopic studies has retrieved increasing interest in recent years. The high gyromagnetic ratio of ^(19)F and its absence in native biomolecular systems make this nucleus an interesting alternative to standard ¹H NMR spectroscopy. Here we show how we can attach a label, carrying a ^(19)F atom, to protein tyrosines, through the use of a specific three component Mannich-type reaction. To validate the efficacy and the...

More...
0 Replies | 108 Views
» Stats
Members: 3,202
Threads: 25,759
Posts: 26,145
Top Poster: nmrlearner (23,203)
Welcome to our newest member, bpadmanabhan
Powered by vBadvanced CMPS v3.2.2

All times are GMT. The time now is 09:38 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