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

		BioNMR > Educational resources > Journal club
[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

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

04-11-2013, 09:27 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

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

Read comments about this paper at Mendeley Biomolecular NMR group

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[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
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy 13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy Abstract Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics of aromatic side chains and its response to biologically relevant events. Indeed, measurements of 13C relaxation rates in aromatic moieties have a long history in biomolecular NMR, primarily in the context of...	nmrlearner	Journal club	0	07-05-2012 04:13 AM
NMR profiling of histone deacetylase and acetyl-transferase activities in real time. NMR profiling of histone deacetylase and acetyl-transferase activities in real time. NMR profiling of histone deacetylase and acetyl-transferase activities in real time. ACS Chem Biol. 2011 May 20;6(5):419-24 Authors: Dose A, Liokatis S, Theillet FX, Selenko P, Schwarzer D Abstract Histone deacetylases (HDACs) and histone acetyl-transferases (HATs) are universal regulators of eukaryotic transcriptional activity and emerging therapeutic targets for human diseases. Here we describe the generation of isotope-labeled deacetylation and...	nmrlearner	Journal club	0	09-07-2011 06:28 PM
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation. Probing Protein Side Chain Dynamics via (13)C NMR Relaxation. Probing Protein Side Chain Dynamics via (13)C NMR Relaxation. Protein Pept Lett. 2011 Jan 11; Authors: Yang D Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...	nmrlearner	Journal club	0	01-13-2011 12:00 PM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. J Am Chem Soc. 2005 Jun 8;127(22):8214-25 Authors: Tugarinov V, Ollerenshaw JE, Kay LE New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc. 2001 Feb 7;123(5):967-75 Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE A new NMR experiment is presented for...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fra Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments. Related Articles Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments. J Protein Chem. 1993 Dec;12(6):695-707 Authors: Huque ME, Vogel HJ The pH-titration and dynamic behaviour of the seven lysine side chains in bovine calmodulin were studied by carbon-13 NMR. The amino groups of the calcium saturated protein and its proteolytic fragments TR1C (1-75) and TR2C (78-148) were dimethylated with carbon-13 labeled...	nmrlearner	Journal club	0	08-22-2010 03:01 AM
arginine side chain assignment pulse wanted Hi, I want use 15N labeling for arginine side chain assignment. it seems the 2D HE(NE)HGHH is the right pulse to use ( J bio. NMR. 10(1997):193 ). You will be very appreciated for any information about getting this pulse. Thanks.	NMR_MSU_LU	NMR Questions and Answers	0	11-17-2006 09:39 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