NMR paper Unfolded proteins and protein folding studied by NMR.

		BioNMR > Educational resources > Journal club
[NMR paper] Unfolded proteins and protein folding studied by NMR.

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

11-24-2010, 10:01 PM

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

Unfolded proteins and protein folding studied by NMR.

Unfolded proteins and protein folding studied by NMR.

Related Articles Unfolded proteins and protein folding studied by NMR.

Chem Rev. 2004 Aug;104(8):3607-22

Authors: Dyson HJ, Wright PE

PMID: 15303830 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins. Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins. Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins. J Biol Chem. 2011 Apr 20; Authors: Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y Co-chaperonin GroES from E. coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i. e., the...	nmrlearner	Journal club	0	04-22-2011 02:00 PM
Comprehensive determination of 3JHNHÎ± for unfolded proteins using 13Câ?²-resolved spin-echo difference spectroscopy Comprehensive determination of 3JHNHÎ± for unfolded proteins using 13Câ?²-resolved spin-echo difference spectroscopy Abstract An experiment is presented to determine 3JHNHÎ± coupling constants, with significant advantages for applications to unfolded proteins. The determination of coupling constants for the peptide chain using 1D 1H, or 2D and 3D 1H-15N correlation spectroscopy is often hampered by extensive resonance overlap when dealing with flexible, disordered proteins. In the experiment detailed here, the overlap problem is largely circumvented by recording 1H-13Câ?² correlation...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15Nâ??1HN cross peaks. For such residues, one cannot unambiguously link the â??leftâ?? side of the NH root to the â??rightâ?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...	nmrlearner	Journal club	0	12-31-2010 08:38 PM
[NMR paper] Millisecond protein folding studied by NMR spectroscopy. Millisecond protein folding studied by NMR spectroscopy. Related Articles Millisecond protein folding studied by NMR spectroscopy. Protein Pept Lett. 2005 Feb;12(2):139-46 Authors: Zeeb M, Balbach J Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] Dynamics in the unfolded state of beta2-microglobulin studied by NMR. Dynamics in the unfolded state of beta2-microglobulin studied by NMR. Related Articles Dynamics in the unfolded state of beta2-microglobulin studied by NMR. J Mol Biol. 2005 Feb 11;346(1):279-94 Authors: Platt GW, McParland VJ, Kalverda AP, Homans SW, Radford SE Many proteins form amyloid-like fibrils in vitro under conditions that favour the population of partially folded conformations or denatured state ensembles. Characterising the structural and dynamic properties of these states is crucial towards understanding the mechanisms of...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy. Protein folding studied by real-time NMR spectroscopy. Related Articles Protein folding studied by real-time NMR spectroscopy. Methods. 2004 Sep;34(1):65-74 Authors: Zeeb M, Balbach J Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct. 1992;21:243-65 Authors: Englander SW, Mayne L HX-labeling experiments in the pH-pulse mode show that protein folding can be remarkably fast. A near-native form can be reached within milliseconds. Experimental analysis of...	nmrlearner	Journal club	0	08-21-2010 11:41 PM
Theoretical framework for NMR residual dipolar couplings in unfolded proteins Theoretical framework for NMR residual dipolar couplings in unfolded proteins O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov Journal of Biomolecular NMR; 2007; 39(1) pp 1-16 Abstract: A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...	stewart	Journal club	0	08-05-2008 02:26 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