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 05-12-2016, 09:30 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 Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR.

Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR.

Related Articles Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR.

Chemphyschem. 2016 May 11;

Authors: Ivancic V, Ekanayake O, Lazo N

Abstract
The mechanism for the interaction of thioflavin T (ThT) with amyloid fibrils at the molecular level is not known. Here, we used ¹H NMR spectroscopy to determine the binding mode of ThT on the surface of fibrils from lysozyme and insulin. Relayed rotating-frame Overhauser enhancements in ThT were observed indicating that the orientation of ThT is orthogonal to the fibril surface. Importantly, the assembly state of ThT on both surfaces is different. On the surface of insulin fibrils, ThT is oligomeric as indicated by rapid ¹H spin-lattice relaxation rate in the rotating frame (R??) presumably due to intermolecular dipole-dipole interactions between ThT molecules. In contrast, ThT on the surface of lysozyme fibrils is a monomer as indicated by slower ¹H R??. These results shed new light into the mechanism for the enhancement of ThT fluorescence and may lead to more efficient detectors of amyloid assemblies which have escaped detection by ThT in monomer form.


PMID: 27165642 [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
[NMR paper] Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Quenched Hydrogen Exchange NMR of Amyloid Fibrils. Related Articles Quenched Hydrogen Exchange NMR of Amyloid Fibrils. Methods Mol Biol. 2016;1345:211-22 Authors: Alexandrescu AT Abstract Amyloid fibrils are associated with a number of human diseases. These aggregatively misfolded intermolecular ?-sheet assemblies constitute some of the most challenging targets in structural biology because to their complexity, size, and insolubility. Here, protocols and controls are described for experiments designed to study hydrogen-bonding in...
nmrlearner Journal club 0 10-12-2015 01:04 AM
[NMR paper] High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR. High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR. J Am Chem Soc. 2015 May 22; Authors: Colvin MT, Silvers R, Frohm B, Su Y, Linse S, Griffin RG Abstract The presence of amyloid plaques composed of amyloid beta (A?) fibrils is a hallmark of Alzheimer's disease (AD). The A? peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted A?1-40 and A?1-42, respectively....
nmrlearner Journal club 0 05-23-2015 10:08 AM
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle. J Biol Chem. 2014 Apr 4;289(14):9998-10010 Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
nmrlearner Journal club 0 05-31-2014 01:57 PM
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif Journal of the American Chemical Society DOI: 10.1021/ja1072178 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
nmrlearner Journal club 0 02-22-2011 11:06 PM
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. J Mol Biol. 2010 Nov 18; Authors: Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A Despite its importance in the context of conformational diseases, structural information is still sparse for protein fibrils. Hydrogen/deuterium exchange measurements of backbone amides allow to identify hydrogen-bonding patterns and reveal pertinent information about...
nmrlearner Journal club 0 11-26-2010 05:32 PM
Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by M
Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR. Related Articles Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR. J Phys Chem B. 2010 Oct 6; Authors: Caporini MA, Bajaj VS, Veshtort M, Fitzpatrick A, Macphee CE, Vendruscolo M, Dobson CM, Griffin RG Amyloid fibrils are structurally ordered aggregates of proteins whose formation is associated with many neurodegenerative and other diseases. For that reason, their high-resolution...
nmrlearner Journal club 0 10-12-2010 02:52 PM
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by So
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy He?le?ne Van Melckebeke, Christian Wasmer, Adam Lange, Eiso AB, Antoine Loquet, Anja Bo?ckmann and Beat H. Meier http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104213j/aop/images/medium/ja-2010-04213j_0001.gif Journal of the American Chemical Society DOI: 10.1021/ja104213j http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/qGRhA6CtOVc
nmrlearner Journal club 0 09-10-2010 12:48 AM
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100864t/aop/images/medium/bi-2010-00864t_0004.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable). More...
nmrlearner Journal club 0 08-18-2010 12:19 AM


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 01:00 PM.


Map