Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone Proteins

		BioNMR > Educational resources > Journal club
Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone 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

08-19-2016, 05:49 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,808

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

Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone Proteins

Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone Proteins

Biochemistry
DOI: 10.1021/acs.biochem.6b00293

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
The Achilles’ Heel of “Ultrastable”Hyperthermophile Proteins: Submillimolar Concentrations of SDS StimulateRapid Conformational Change, Aggregation, and Amyloid Formation inProteins Carrying Overall Positive Charge The Achilles’ Heel of “Ultrastable”Hyperthermophile Proteins: Submillimolar Concentrations of SDS StimulateRapid Conformational Change, Aggregation, and Amyloid Formation inProteins Carrying Overall Positive Charge http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01343/20160706/images/medium/bi-2015-013433_0011.gif Biochemistry DOI: 10.1021/acs.biochem.5b01343 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/eNvtvqsdbN0 More...	nmrlearner	Journal club	0	07-07-2016 04:21 AM
[NMR paper] Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Related Articles Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Proc Natl Acad Sci U S A. 2015 Jun 29; Authors: Libich DS, Tugarinov V, Clore GM Abstract The prototypical chaperonin GroEL assists protein folding through an ATP-dependent encapsulation mechanism. The details of how GroEL folds proteins remain elusive,...	nmrlearner	Journal club	0	07-01-2015 02:40 PM
Recombinant proteins incorporating short non-native extensions may display increased aggregation propensity as detected by high resolution NMR spectroscopy Recombinant proteins incorporating short non-native extensions may display increased aggregation propensity as detected by high resolution NMR spectroscopy 26 October 2012 Publication year: 2012 Source:Biochemical and Biophysical Research Communications, Volume 427, Issue 3</br> </br> The use of a recombinant protein to investigate the function of the native molecule requires that the former be obtained with the same amino acid sequence as the template. However, in many cases few additional residues are artificially introduced for cloning or purification purposes,...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach. Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach. Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach. Curr Protein Pept Sci. 2011 Feb 24; Authors: Orcellet ML, Fernández CO The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a...	nmrlearner	Journal club	0	02-26-2011 11:56 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...	nmrlearner	Journal club	0	01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. J Biomol NMR. 2011 Jan 21; Authors: Etzkorn M, Böckmann A, Baldus M It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...	nmrlearner	Journal club	0	01-22-2011 01:52 PM
Probing the micelle-bound aggregation-prone state of ?-synuclein with (19)F NMR spectroscopy. Probing the micelle-bound aggregation-prone state of ?-synuclein with (19)F NMR spectroscopy. Probing the micelle-bound aggregation-prone state of ?-synuclein with (19)F NMR spectroscopy. Chembiochem. 2010 Sep 24;11(14):1993-6 Authors: Wang GF, Li C, Pielak GJ	nmrlearner	Journal club	0	01-21-2011 01:22 AM
[NMR paper] The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliat The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures. Related Articles The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures. Structure. 2002 May;10(5):673-86 Authors: Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray...	nmrlearner	Journal club	0	11-24-2010 08:49 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