New analysis shows how proteins shift into working mode - R & D Magazine

		BioNMR > NMR community > Online News
New analysis shows how proteins shift into working mode - R & D Magazine

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

08-08-2013, 03:46 PM

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

New analysis shows how proteins shift into working mode - R & D Magazine

New analysis shows how proteins shift into working mode - R & D Magazine

R & D Magazine

New analysis shows how proteins shift into working mode
R & D Magazine
One, cyclophilin A, can facilitate protein folding, while the other, dihydrofolate reductase (dhfr), helps regulate cell proliferation and cell growth. Their method, for the first time, provides an atomically detailed structural framework for the dhfr ...

Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
The hungry bypass veggies for starches, proteins - R & D Magazine The hungry bypass veggies for starches, proteins - R & D Magazine <img alt="" height="1" width="1" /> The hungry bypass veggies for starches, proteins R & D Magazine People coming off 18-hour fasts are more likely to opt for a starchy food or a protein instead of more healthful vegetables, finds a new study. ... JEOL to launch world's smallest solid-state NMR probe. Apr 12. According to JEOL Resonance, a new ... Read here	nmrlearner	Online News	0	07-07-2012 10:16 PM
Researchers develop way to strengthen proteins with polymers - R & D Magazine Researchers develop way to strengthen proteins with polymers - R & D Magazine http://www.bionmr.com//nt1.ggpht.com/news/tbn/1e8ZLQCvJy_rwM/6.jpg Azom.com <img alt="" height="1" width="1" /> Researchers develop way to strengthen proteins with polymers R & D Magazine Proteins are widely used as drugsâ??insulin for diabetics is the best known ... next week of a new 0.75-mm solid state nuclear magnetic resonance (NMR) probe. Polymers Can be Used to Stabilize ProteinsAzom.com	nmrlearner	Online News	0	06-13-2012 11:34 AM
4D Non-uniformly sampled HCBCACON and 1J(NCÎ±)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins 4D Non-uniformly sampled HCBCACON and 1J(NCÎ±)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (HÎ±, and HÎ²) and carbon (CÎ±, CÎ²) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient...	nmrlearner	Journal club	0	05-17-2012 08:40 AM
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins Abstract Zinc is the second most abundant metal ion incorporated in proteins, and is in many cases a crucial component of protein three-dimensional structures. Zinc ions are frequently coordinated by cysteine and histidine residues. Whereas cysteines bind to zinc via their unique SÎ³ atom, histidines can coordinate zinc with two different coordination modes, either NÎ´1 or NÎµ2 is coordinating the zinc ion. The determination of this coordination mode is crucial for the accurate...	nmrlearner	Journal club	0	04-23-2012 03:31 AM
A New Tool to Reveal Structure of Proteins - Lab Manager Magazine A New Tool to Reveal Structure of Proteins - Lab Manager Magazine <img alt="" height="1" width="1" /> A New Tool to Reveal Structure of Proteins Lab Manager Magazine For roughly a decade, a technique called solid state nuclear magnetic resonance (NMR) spectroscopy has allowed researchers to detect the arrangements of atoms in proteins that defy study by traditional laboratory tools such as X-ray crystallography. and more » Read here	nmrlearner	Online News	0	03-20-2012 10:52 PM
[NMR paper] NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure. Related Articles NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure. J Biol Chem. 2004 Apr 9;279(15):15177-82 Authors: Wain R, Redfield C, Ferguson SJ, Smith LJ Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] A structural mode-coupling approach to 15N NMR relaxation in proteins. A structural mode-coupling approach to 15N NMR relaxation in proteins. Related Articles A structural mode-coupling approach to 15N NMR relaxation in proteins. J Am Chem Soc. 2001 Apr 4;123(13):3055-63 Authors: Tugarinov V, Liang Z, Shapiro YE, Freed JH, Meirovitch E The two-body Slowly Relaxing Local Structure (SRLS) model was applied to (15)N NMR spin relaxation in proteins and compared with the commonly used original and extended model-free (MF) approaches. In MF, the dynamic modes are assumed to be decoupled, local ordering at the N-H sites...	nmrlearner	Journal club	0	11-19-2010 08:32 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