NMR paper Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.

		BioNMR > Educational resources > Journal club
[NMR paper] Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.

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

Rating:

Display Modes

02-03-2013, 10:19 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,734

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

Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.

Related Articles Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.

Chem Commun (Camb). 2013 Jan 29;

Authors: Taylor SL, Crawley-Snowdon H, Wagstaff JL, Rowe ML, Shepherd M, Williamson RA, Howard MJ

Abstract
NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple (15)N HSQC protein resonances across a titration series using mixtures of oxidised and reduced glutathione. Results for PDI a, PDI ab and DsbA agree with the literature and our result for ERp18 confirms this protein as an oxidoreductase of comparable or greater reducing strength than PDI a.

PMID: 23360928 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release) DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release) <img alt="" height="1" width="1" /> DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking 7thSpace Interactive (press release) Unfortunately, the experimental determination of protein-RNA complexes is tedious and difficult, both by X-ray crystallography and NMR. For many interacting proteins and RNAs the individual structures are available, enabling computational prediction of ... Read here	nmrlearner	Online News	0	08-19-2011 04:02 AM
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. J Biomol NMR. 2011 Mar 18; Authors: Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange...	nmrlearner	Journal club	0	03-23-2011 05:41 PM
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...	nmrlearner	Journal club	0	03-22-2011 07:32 PM
[NMR paper] Validating the use of database potentials in protein structure determination by NMR. Validating the use of database potentials in protein structure determination by NMR. Related Articles Validating the use of database potentials in protein structure determination by NMR. FEBS Lett. 2005 Oct 24;579(25):5542-8 Authors: Mertens HD, Gooley PR The refinement of protein structures determined by nuclear magnetic resonance spectroscopy against database potentials of mean force allows for the exclusion of unfavourable conformations of the protein backbone during a structure calculation, resulting in protein structures with a marked...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
An introduction to NMR-based approaches for measuring protein dynamics. An introduction to NMR-based approaches for measuring protein dynamics. An introduction to NMR-based approaches for measuring protein dynamics. Biochim Biophys Acta. 2010 Nov 5; Authors: Kleckner IR, Foster MP Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the...	nmrlearner	Journal club	0	11-10-2010 02:29 PM
NMR-based protein potentials. NMR-based protein potentials. More...	nmrlearner	General	0	10-14-2010 05:01 PM
[NMR paper] Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: appl Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2. Related Articles Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2. J Biomol NMR. 1995 Nov;6(3):321-8 Authors: Dingley AJ, Mackay JP, Chapman BE, Morris MB, Kuchel PW, Hambly BD, King GF At the millimolar concentrations required for structural studies, NMR spectra of the calcium-binding protein myosin light chain 2 (MLC2) showed resonance line widths indicative...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
NMR-Based Protein Potentials. NMR-Based Protein Potentials. Related Articles NMR-Based Protein Potentials. Angew Chem Int Ed Engl. 2010 Aug 16; Authors: Li DW, BrÃ¼schweiler R	nmrlearner	Journal club	0	08-18-2010 11:15 AM

« 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