NMR paper The utility of small nutation angle (1)H pulses for NMR studies of methyl-containing side-chain dynamics in proteins

		BioNMR > Educational resources > Journal club
[NMR paper] The utility of small nutation angle (1)H pulses for NMR studies of methyl-containing side-chain dynamics in proteins

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

12-08-2024, 06:06 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,776

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

The utility of small nutation angle (1)H pulses for NMR studies of methyl-containing side-chain dynamics in proteins

The utility of small nutation angle (1)H pulses for NMR studies of methyl-containing side-chain dynamics in proteins

We describe the utility of small nutation angle (acute;

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Side-Chain Dynamics of the ?1B-Adrenergic Receptor determined by NMR via Methyl Relaxation Side-Chain Dynamics of the ?1B-Adrenergic Receptor determined by NMR via Methyl Relaxation Abstract G protein-coupled receptors (GPCRs) are medically important membrane proteins that sample inactive, intermediate, and active conformational states characterized by relatively slow interconversions (~?s–ms). On a faster timescale (~ps–ns), the conformational landscape of GPCRs is governed by the rapid dynamics of amino acid side chains. Such dynamics are essential for protein functions such as ligand recognition and allostery. Unfortunately, technical challenges have almost entirely...	nmrlearner	Journal club	0	10-09-2023 04:39 PM
[NMR paper] Side-Chain Dynamics of the ?1B -Adrenergic Receptor determined by NMR via Methyl Relaxation Side-Chain Dynamics of the ?1B -Adrenergic Receptor determined by NMR via Methyl Relaxation G protein-coupled receptors (GPCRs) are medically important membrane proteins that sample inactive, intermediate, and active conformational states characterized by relatively slow interconversions (~?s-ms). On a faster timescale (~ps-ns), the conformational landscape of GPCRs is governed by the rapid dynamics of amino acid side chains. Such dynamics are essential for protein functions such as ligand recognition and allostery. Unfortunately, technical challenges have almost entirely precluded the......	nmrlearner	Journal club	0	10-09-2023 04:39 PM
[NMR paper] Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial...	nmrlearner	Journal club	0	02-17-2022 11:34 AM
[ASAP] Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation Xinyao Xiang, Alexandar L. Hansen, Lei Yu, Gregory Jameson, Lei Bruschweiler-Li, Chunhua Yuan, and Rafael Bru?schweiler https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c04687/20210824/images/medium/ja1c04687_0005.gif Journal of the American Chemical Society DOI: 10.1021/jacs.1c04687 http://feeds.feedburner.com/~r/acs/jacsat/~4/8joQZH1-cyY	nmrlearner	Journal club	0	08-26-2021 06:47 AM
[NMR paper] Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation Amino-acid side-chain properties in proteins are key determinants of protein function. NMR spin relaxation of side chains is an important source of information about local protein dynamics and flexibility. However, traditional solution NMR relaxation methods are most sensitive to sub-nanosecond dynamics lacking information on slower ns-?s time-scale motions. Nanoparticle-assisted NMR spin relaxation (NASR) of methyl-side chains is introduced here as a window into these ns-?s...	nmrlearner	Journal club	0	08-26-2021 06:47 AM
[NMR paper] The Measurement of Relaxation Rates of Degenerate 1H Transitions in Methyl Groups of Proteins Using Acute Angle Radiofrequency Pulses The Measurement of Relaxation Rates of Degenerate 1H Transitions in Methyl Groups of Proteins Using Acute Angle Radiofrequency Pulses Publication date: Available online 14 July 2021 Source: Journal of Magnetic Resonance Author(s): Vitali Tugarinov, G. Marius Clore	nmrlearner	Journal club	0	07-14-2021 10:07 PM
[NMR paper] Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups The dynamics of methyl-bearing side chains in proteins were probed by ^(13)C relaxation measurements of a number of ^(13)C magnetization modes in selectively ^(13)CH(3)-labeled methyl groups of proteins. We first show how ^(13)C magnetization modes in a ^(13)CH(3) spin-system can be isolated using acute-angle ¹H radio-frequency pulses. The parameters of methyl-axis dynamics, a measure of methyl-axis ordering (S(axis)²) and the correlation time of fast local methyl-axis...	nmrlearner	Journal club	0	03-27-2021 02:09 AM
NMR Relaxation and Molecular Dynamics Simulations of Side Chain Dynamics in Proteins NMR Relaxation and Molecular Dynamics Simulations of Side Chain Dynamics in Proteins Publication date: 2 February 2018 Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br> Author(s): Falk Hoffmann, Mengjun Xue, Frans Mulder, Lars Schäfer</br> </br></br> </br></br> More...	nmrlearner	Journal club	0	02-07-2018 03:41 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off