NMR paper Toward optimal-resolution NMR of intrinsically disordered proteins.

		BioNMR > Educational resources > Journal club
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.

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

03-25-2014, 11:49 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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

Toward optimal-resolution NMR of intrinsically disordered proteins.

Toward optimal-resolution NMR of intrinsically disordered proteins.

Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins.

J Magn Reson. 2014 Apr;241:41-52

Authors: Nová?ek J, Zídek L, Sklená? V

Abstract
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular processes, there is an urgent need to characterize the conformational behavior of IDPs at the highest possible level. The unique feature of NMR spectroscopy in the context of IDPs is its ability to supply details of their structural and temporal alterations at atomic-level resolution. Here, we briefly review recently proposed NMR-based strategies to characterize transient states populated by IDPs and summarize the latest achievements and future prospects in methodological development. Because low chemical shift dispersion represents the major obstacle encountered when studying IDPs by nuclear magnetic resonance, particular attention is paid to techniques allowing one to approach the physical limits of attainable resolution.

PMID: 24656079 [PubMed - in process]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Toward optimal-resolution NMR of intrinsically disordered proteins Toward optimal-resolution NMR of intrinsically disordered proteins Publication date: April 2014 Source:Journal of Magnetic Resonance, Volume 241</br> Author(s): Ji?í Nová?ek , Lukáš Žídek , Vladimír Sklená?</br> Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular...	nmrlearner	Journal club	0	03-21-2014 12:52 AM
[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling. Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling. Related Articles Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling. Chem Commun (Camb). 2013 Dec 23; Authors: Helge Meyer N, Zangger K Abstract Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear...	nmrlearner	Journal club	0	12-25-2013 03:39 PM
[NMR paper] Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering. Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering. Related Articles Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering. Structure. 2013 Dec 18; Authors: Schwalbe M, Ozenne V, Bibow S, Jaremko M, Jaremko L, Gajda M, Jensen MR, Biernat J, Becker S, Mandelkow E, Zweckstetter M, Blackledge M Abstract The development of molecular descriptions of intrinsically...	nmrlearner	Journal club	0	12-24-2013 01:04 PM
[NMR paper] Structural characterization of intrinsically disordered proteins by NMR spectroscopy. Structural characterization of intrinsically disordered proteins by NMR spectroscopy. Structural characterization of intrinsically disordered proteins by NMR spectroscopy. Molecules. 2013;18(9):10802-28 Authors: Kosol S, Contreras-Martos S, Cedeño C, Tompa P Abstract Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and intrinsically disordered...	nmrlearner	Journal club	0	09-07-2013 09:54 PM
[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR. Describing intrinsically disordered proteins at atomic resolution by NMR. Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR. Curr Opin Struct Biol. 2013 Mar 29; Authors: Jensen MR, Ruigrok RW, Blackledge M Abstract There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...	nmrlearner	Journal club	0	04-03-2013 08:22 PM
Describing intrinsically disordered proteins at atomic resolution by NMR Describing intrinsically disordered proteins at atomic resolution by NMR Available online 29 March 2013 Publication year: 2013 Source:Current Opinion in Structural Biology</br> </br> There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...	nmrlearner	Journal club	0	03-29-2013 07:52 PM
Intrinsically disordered proteins - PhysicsToday.org Intrinsically disordered proteins - PhysicsToday.org <img alt="" height="1" width="1" /> Intrinsically disordered proteins PhysicsToday.org Indeed, much of the community's understanding of protein function rests on our ability to deduce those structures by such methods as x-ray crystallography and nuclear magnetic resonance (NMR). The immense success and explanatory power of the ... Read here	nmrlearner	Online News	0	08-01-2012 09:35 PM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using Î´ subunit (20 kDa) of Bacillus subtilis RNA polymerase...	nmrlearner	Journal club	0	02-21-2012 03:40 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