[ASAP] Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein

		BioNMR > Educational resources > Journal club
[ASAP] Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein

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

12-04-2020, 03:46 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

[ASAP] Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein

[ASAP] Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein

Biochemistry
DOI: 10.1021/acs.biochem.0c00721

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Related Articles Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Sci Rep. 2020 Nov 11;10(1):19574 Authors: Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S Abstract Using SAXS and NMR spectroscopy, we herein provide a high-resolution description of the intrinsically disordered N-terminal...	nmrlearner	Journal club	0	11-13-2020 04:07 PM
[ASAP] Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET Gregory-Neal W. Gomes, Mickae?l Krzeminski, Ashley Namini, Erik W. Martin, Tanja Mittag, Teresa Head-Gordon, Julie D. Forman-Kay, and Claudiu C. Gradinaru https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c02088/20200904/images/medium/ja0c02088_0006.gif Journal of the American Chemical Society DOI: 10.1021/jacs.0c02088 http://feeds.feedburner.com/~r/acs/jacsat/~4/ouvFj6sHuyQ	nmrlearner	Journal club	0	09-13-2020 09:18 AM
[ASAP] Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00056/20180423/images/medium/bi-2018-00056k_0005.gif Biochemistry DOI: 10.1021/acs.biochem.8b00056 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/Y2hdVN8M2dU More...	nmrlearner	Journal club	0	04-24-2018 01:29 PM
[ASAP] Structural Regulation of a Neurofilament-Inspired Intrinsically Disordered Protein Brush by Multisite Phosphorylation Structural Regulation of a Neurofilament-Inspired Intrinsically Disordered Protein Brush by Multisite Phosphorylation https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00007/20180405/images/medium/bi-2018-00007d_0006.gif Biochemistry DOI: 10.1021/acs.biochem.8b00007 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/F1MKHnlpmnA More...	nmrlearner	Journal club	0	04-07-2018 03:45 AM
[NMR paper] NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B. NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B. Related Articles NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B. J Biol Chem. 2017 Sep 14;: Authors: Bessa LM, Launay H, Dujardin M, Cantrelle FX, Lippens G, Landrieu I, Schneider R, Hanoulle X Abstract Non-structural protein 5B (NS5B) is the RNAdependent RNA polymerase that catalyses replication of the...	nmrlearner	Journal club	0	09-16-2017 09:58 PM
Engineering Aromatic–Aromatic InteractionsTo Nucleate Folding in Intrinsically Disordered Regions of Proteins Engineering Aromatic–Aromatic InteractionsTo Nucleate Folding in Intrinsically Disordered Regions of Proteins http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00437/20170810/images/medium/bi-2017-00437t_0014.gif Biochemistry DOI: 10.1021/acs.biochem.7b00437 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/wmlprcVf3bg More...	nmrlearner	Journal club	0	08-11-2017 08:52 PM
Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500904f/20141007/images/medium/bi-2014-00904f_0012.gif Biochemistry DOI: 10.1021/bi500904f http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/uw_59WsXyRU More...	nmrlearner	Journal club	0	10-08-2014 04:17 AM
[NMR paper] The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. Related Articles The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. Biochemistry. 2014 Sep 10; Authors: Xue Y, Yuwen T, Zhu F, Skrynnikov NR Abstract ...	nmrlearner	Journal club	0	09-11-2014 02:54 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