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 04-03-2018, 05:04 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 19,916
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 [ASAP] Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein

[ASAP] Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein



Biochemistry
DOI: 10.1021/acs.biochem.8b00002



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.
Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes. Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes. Sci Rep. 2017 Apr 07;7:46128 Authors: Schrottke S, Kaiser A, Vortmeier G, Els-Heindl S, Worm D, Bosse M, Schmidt P, Scheidt HA, Beck-Sickinger AG, Huster D Abstract The expression, functional reconstitution and first NMR characterization of the human growth...
nmrlearner Journal club 0 04-08-2017 10:57 AM
Functional Analysis of a Bacterial Antifreeze Protein Indicates a Cooperative Effect between Its Two Ice-Binding Domains
Functional Analysis of a Bacterial Antifreeze Protein Indicates a Cooperative Effect between Its Two Ice-Binding Domains http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00323/20160708/images/medium/bi-2016-00323b_0009.gif Biochemistry DOI: 10.1021/acs.biochem.6b00323 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/TcySP41w7g8 More...
nmrlearner Journal club 0 07-10-2016 10:50 AM
[NMR paper] Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue.
Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue. Related Articles Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue. Biochem Biophys Res Commun. 2016 Jun 24; Authors: Alsanousi N, Sugiki T, Furuita K, So M, Lee YH, Fujiwara T, Kojima C Abstract Humanin comprising 24 amino acid residues is a bioactive peptide that has been isolated from the brain tissue of patients with...
nmrlearner Journal club 0 06-30-2016 02:26 AM
[NMR paper] Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation. Related Articles Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation. Proc Natl Acad Sci U S A. 2016 Jun 13; Authors: Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C Abstract Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of...
nmrlearner Journal club 0 06-15-2016 11:12 PM
[NMR paper] A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes. Biophys J. 2013 Nov 19;105(10):2333-42 Authors: Kwon B, Waring AJ, Hong M Abstract Domain formation in bacteria-mimetic membranes...
nmrlearner Journal club 0 07-12-2014 04:28 AM
[NMR paper] Potent ?-secretase inhibitors/modulators interact with Amyloid-? fibrils but do not inhibit fibrillation: A high-resolution NMR study.
Potent ?-secretase inhibitors/modulators interact with Amyloid-? fibrils but do not inhibit fibrillation: A high-resolution NMR study. Related Articles Potent ?-secretase inhibitors/modulators interact with Amyloid-? fibrils but do not inhibit fibrillation: A high-resolution NMR study. Biochem Biophys Res Commun. 2014 Apr 16; Authors: Yesuvadian R, Krishnamoorthy J, Ramamoorthy A, Bhunia A Abstract Recently, ?-secretase modulators (GSM) have been shown to interact directly with the amyloid precursor protein (APP) and...
nmrlearner Journal club 0 04-22-2014 03:54 PM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies. Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies. Protein Expr Purif. 2011 Feb 11; Authors: Wang X, Gill Jr RL, Zhu Q, Tian F LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
nmrlearner Journal club 0 02-16-2011 07:40 PM
(31)P NMR and AFM studies on the destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109.
(31)P NMR and AFM studies on the destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109. Related Articles (31)P NMR and AFM studies on the destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109. IUBMB Life. 2010 Nov;62(11):841-51 Authors: Damai RS, Sankhala RS, Anbazhagan V, Swamy MJ The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by...
nmrlearner Journal club 0 12-01-2010 04:41 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 - 2020, 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 10:56 AM.


Map