Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding | Communications Biology - Nature.com

		BioNMR > NMR community > Online News
Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding \| Communications Biology - Nature.com

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

06-23-2022, 06:33 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,775

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

Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding | Communications Biology - Nature.com

Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding | Communications Biology - Nature.com

Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding | Communications Biology Nature.com Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Artificial intelligence guided conformational mining of intrinsically disordered proteins \| Communications Biology - Nature.com Artificial intelligence guided conformational mining of intrinsically disordered proteins \| Communications Biology - Nature.com Artificial intelligence guided conformational mining of intrinsically disordered proteins \| Communications Biology Nature.com Read here	nmrlearner	Online News	0	06-23-2022 06:33 AM
Peptidoglycan maturation controls outer membrane protein assembly - Nature.com Peptidoglycan maturation controls outer membrane protein assembly - Nature.com Peptidoglycan maturation controls outer membrane protein assembly Nature.com Read here	nmrlearner	Online News	0	06-17-2022 09:21 PM
Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs \| Communications Biology - Nature.com Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs \| Communications Biology - Nature.com Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs \| Communications Biology Nature.com Read here	nmrlearner	Online News	0	04-30-2022 05:19 AM
[ASAP] Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00195/20210601/images/medium/bi1c00195_0006.gif Biochemistry DOI: 10.1021/acs.biochem.1c00195 http://feeds.feedburner.com/~r/acs/bichaw/~4/8DFN1W6q71s More...	nmrlearner	Journal club	0	06-01-2021 11:42 PM
Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01153/20161214/images/medium/bi-2016-01153h_0016.gif Biochemistry DOI: 10.1021/acs.biochem.6b01153 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/Gp7LZ32EIRs More...	nmrlearner	Journal club	0	12-15-2016 06:49 PM
Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ... - Nature.com Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ... - Nature.com <img alt="" height="1" width="1"> Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ... Nature.com Solid-state NMR and fluorescence spectroscopy data show that ssDNA binds PLN's cytoplasmic domain specifically, but does not affect SERCA in the absence of the regulatory protein. In particular, NMR spectra show that ssDNA shifts the conformational ... Read here	nmrlearner	Online News	0	08-24-2015 06:42 PM
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A 22 February 2012 Publication year: 2012 Source:Biophysical Journal, Volume 102, Issue 4</br> </br> Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
[NMR paper] NMR solution structure of the periplasmic chaperone FimC. NMR solution structure of the periplasmic chaperone FimC. Related Articles NMR solution structure of the periplasmic chaperone FimC. Nat Struct Biol. 1998 Oct;5(10):885-90 Authors: Pellecchia M, Güntert P, Glockshuber R, Wüthrich K The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC...	nmrlearner	Journal club	0	11-17-2010 11:15 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