BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 04-30-2019, 03:58 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,137
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default NMR structure of a full-length single-pass membrane protein NRADD.

NMR structure of a full-length single-pass membrane protein NRADD.

Related Articles NMR structure of a full-length single-pass membrane protein NRADD.

Proteins. 2019 Apr 29;:

Authors: Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS

Abstract
Structural study of any single-pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor-alike death-domain protein, NRADD. The structure and dynamics of the protein was investigated by conventional nuclear magnetic resonance techniques in the solution of phospholipid bicelles. The receptor contains two folded regions - ?-helical transmembrane domain and globular C-terminal death domain with more than 50% of the rest of backbone being disordered. This is the first structure of a full-length single-pass membrane receptor-alike protein solved by the single method. This article is protected by copyright. All rights reserved.


PMID: 31033000 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00995/20171211/images/medium/bi-2017-00995a_0005.gif Biochemistry DOI: 10.1021/acs.biochem.7b00995 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/IYVe61xDFY0 More...
nmrlearner Journal club 0 12-12-2017 02:12 AM
[NMR paper] Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein. Related Articles Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein. Nat Struct Mol Biol. 2016 Mar 28; Authors: Tuttle MD, Comellas G, Nieuwkoop AJ, Covell DJ, Berthold DA, Kloepper KD, Courtney JM, Kim JK, Barclay AM, Kendall A, Wan W, Stubbs G, Schwieters CD, Lee VM, George JM, Rienstra CM Abstract Misfolded ?-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of...
nmrlearner Journal club 0 03-29-2016 04:59 PM
[NMR paper] Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Solid-state NMR of a protein in a precipitated complex with a full-length antibody. Solid-state NMR of a protein in a precipitated complex with a full-length antibody. J Am Chem Soc. 2014 Nov 10; Authors: Lamley JM, Iuga D, Oster C, Sass HJ, Rogowski M, Oss A, Past J, Reinhold A, Grzesiek S, Samoson A, Lewandowski JR Abstract NMR is a prime technique for characterizing atomic resolution structures and dynamics of biomolecular complexes but, for such systems, faces challenges of sensitivity and spectral resolution. We...
nmrlearner Journal club 0 11-11-2014 11:57 AM
NMR Analyses of the Structure and Dynamics of Klebsiella Pneumoniae OMPA Domains and Full Length Protein
NMR Analyses of the Structure and Dynamics of Klebsiella Pneumoniae OMPA Domains and Full Length Protein Publication date: 28 January 2014 Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br> Author(s): Guillaume Nars , Iordan Iordanov , Marie Renault , Olivier Saurel , Pascal Demange , Alain Milon</br> </br></br> </br></br> More...
nmrlearner Journal club 0 01-29-2014 12:50 AM
[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy. Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy. Sci Rep. 2013 Aug 29;3:2538 Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A Abstract Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
nmrlearner Journal club 0 08-30-2013 04:35 PM
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment Abstract Targeting the receptor for the advanced glycation endproducts (RAGE) signalling has a potential for the prevention and treatment of several pathologies. Extracellular activation of RAGE triggers the interactions of the RAGE cytoplasmic tail with intracellular protein partners. Here the cytoplasmic tail of RAGE has been investigated by NMR as part of the full-length protein, in the presence of a membrane-mimicking environment. The isolated cytoplasmic tail has also been studied...
nmrlearner Journal club 0 09-24-2012 01:02 AM
[NMR paper] NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima. Related Articles NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima. J Biomol NMR. 2003 Feb;25(2):163-4 Authors: Ilin S, Hoskins A, Schwalbe H, Wöhnert J
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 1997 Aug 18;413(2):282-8 Authors: Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously...
nmrlearner Journal club 0 08-22-2010 05:08 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 01:13 PM.


Map