Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy - Nature.com

		BioNMR > NMR community > Online News
Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy - Nature.com

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

12-28-2023, 10:50 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy - Nature.com

Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy - Nature.com

Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy Nature.com Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Methodological advancements for characterising protein side chains by NMR spectroscopy Methodological advancements for characterising protein side chains by NMR spectroscopy The surface of proteins is covered by side chains of polar amino acids that are imperative for modulating protein functionality through the formation of noncovalent intermolecular interactions. However, despite their tremendous importance, the unique structures of protein side chains require tailored approaches for investigation by nuclear magnetic resonance spectroscopy and so have traditionally been understudied compared with the protein backbone. Here, we review substantial recent... More...	nmrlearner	Journal club	0	05-16-2021 02:19 AM
[NMR paper] Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy. Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy. Related Articles Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy. Nat Commun. 2019 Apr 15;10(1):1747 Authors: Pritchard RB, Hansen DF Abstract Side chains cover protein surfaces and are fundamental to processes as diverse as substrate recognition, protein folding and enzyme catalysis. However, characterisation of side-chain motions has so far been restricted to small proteins and methyl-bearing side...	nmrlearner	Journal club	0	04-17-2019 01:41 PM
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Chem Commun (Camb). 2017 Aug 25;: Authors: Gerecht K, Figueiredo AM, Hansen DF Abstract Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...	nmrlearner	Journal club	0	08-26-2017 03:38 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The bibliography manager for researchers	nmrlearner	Journal club	0	09-29-2015 02:39 PM
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7 Authors: Werbeck ND, Kirkpatrick J,...	nmrlearner	Journal club	0	01-29-2014 02:01 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The reference manager for researchers	nmrlearner	Journal club	0	10-17-2013 12:49 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The reference manager for researchers	nmrlearner	Journal club	0	04-11-2013 09:27 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The library management tool for researchers	nmrlearner	Journal club	0	04-11-2013 03:08 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