ReAsH as a Quantitative Probe of In-Cell Protein Dynamics

		BioNMR > Educational resources > Journal club
ReAsH as a Quantitative Probe of In-Cell Protein Dynamics

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

03-18-2016, 05:23 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,175

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

ReAsH as a Quantitative Probe of In-Cell Protein Dynamics

ReAsH as a Quantitative Probe of In-Cell Protein Dynamics

Biochemistry
DOI: 10.1021/acs.biochem.5b01336

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Understanding macromolecular crowding is critical for quantitative cell biology - SPIE Newsroom http://www.bionmr.com//t1.gstatic.com/images?q=tbn:ANd9GcSFrZf31PUTVUTveakwA0E1nnJQ316UwMtUs4Y6ZDGqaBp0wkfIb8wo1Lsfi2ZHN1FLVa2FPOY SPIE Newsroom <img alt="" height="1" width="1"> Understanding macromolecular crowding is critical for quantitative cell biology SPIE Newsroom In the past, nuclear magnetic resonance (NMR) has been used to study protein-crowded environments and to investigate the translational and rotational diffusion of chymotrypsin inhibitor 2 in crowded environments. It was found that the heterogeneity of ... Understanding macromolecular crowding is critical for...	nmrlearner	Online News	0	12-15-2015 07:47 AM
Understanding macromolecular crowding is critical for quantitative cell biology - SPIE Newsroom http://www.bionmr.com//t1.gstatic.com/images?q=tbn:ANd9GcSFrZf31PUTVUTveakwA0E1nnJQ316UwMtUs4Y6ZDGqaBp0wkfIb8wo1Lsfi2ZHN1FLVa2FPOY SPIE Newsroom <img alt="" height="1" width="1"> Understanding macromolecular crowding is critical for quantitative cell biology SPIE Newsroom In the past, nuclear magnetic resonance (NMR) has been used to study protein-crowded environments and to investigate the translational and rotational diffusion of chymotrypsin inhibitor 2 in crowded environments. It was found that the heterogeneity of ... Understanding macromolecular crowding is critical for...	nmrlearner	Online News	0	12-12-2015 03:39 AM
[NMR paper] Beyond a fluorescent probe: Inhibition of cell division protein FtsZ by mant-GTP elucidated by NMR and biochemical approaches. Beyond a fluorescent probe: Inhibition of cell division protein FtsZ by mant-GTP elucidated by NMR and biochemical approaches. Related Articles Beyond a fluorescent probe: Inhibition of cell division protein FtsZ by mant-GTP elucidated by NMR and biochemical approaches. ACS Chem Biol. 2015 Aug 6; Authors: Huecas S, Marcelo F, Perona A, Ruiz LB, Morreale A, Cañada FJ, Jimenez-Barbero J, Andreu JM Abstract FtsZ is the organizer of cell division in most bacteria and a target in the quest for new antibiotics. FtsZ is a tubulin-like...	nmrlearner	Journal club	0	08-08-2015 12:17 PM
[NMR paper] Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR. Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR. Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR. Chem Commun (Camb). 2013 Feb 26; Authors: Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, Ariyoshi M, Tochio H, Shirakawa M, Hamachi I Abstract Here we describe how a (19)F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with...	nmrlearner	Journal club	0	02-27-2013 06:47 PM
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics. Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics. Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics. Top Curr Chem. 2011 Sep 7; Authors: Ishima R Abstract Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...	nmrlearner	Journal club	0	09-08-2011 06:50 PM
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy. Related Articles Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy. J Am Chem Soc. 2010 Oct 26; Authors: Schanda P, Meier BH, Ernst M Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin...	nmrlearner	Journal club	0	10-29-2010 07:05 PM
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy Paul Schanda, Beat H. Meier and Matthias Ernst http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja100726a/aop/images/medium/ja-2010-00726a_0001.gif Journal of the American Chemical Society DOI: 10.1021/ja100726a http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/vMvBmzNs148	nmrlearner	Journal club	0	10-26-2010 08:48 PM
A new spin probe of protein dynamics A new spin probe of protein dynamics: nitrogen relaxation in (15)n-(2)h amide groups. Xu J, Millet O, Kay LE, Skrynnikov NR. Contribution from the Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, and Departments of Medical Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada. J Am Chem Soc. 2005 Mar 9;127(9):3220-9. (15)N spin relaxation data have provided a wealth of information on protein dynamics in solution. Standard R(1), R(1)(rho), and NOE experiments aimed at (15)N amide moieties are complemented in this...	nmrlearner	Journal club	0	03-09-2005 06:09 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