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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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  
Old 02-06-2017, 11:28 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
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 Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.

Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.

Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.

J Biomol NMR. 2017 Feb 04;:

Authors: Bauer T, Dotta C, Balacescu L, Gath J, Hunkeler A, Böckmann A, Meier BH

Abstract
The temperature-dependent resonance-line broadening of HET-s(218-289) in its amyloid form is investigated in the range between 110*K and 280*K. Significant differences are observed between residues in the structured hydrophobic triangular core, which are broadened the least and can be detected down to 100*K, and in the solvent-exposed parts, which are broadened the most and often disappear from the observed spectrum around 200*K. Below the freezing of the bulk water, around 273*K, the protein fibrils are still surrounded by a layer of mobile water whose thickness decreases with temperature, leading to drying out of the fibrils.


PMID: 28161758 [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
Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils
Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils Abstract The temperature-dependent resonance-line broadening of HET-s(218â??289) in its amyloid form is investigated in the range between 110Â*K and 280Â*K. Significant differences are observed between residues in the structured hydrophobic triangular core, which are broadened the least and can be detected down to 100Â*K, and in the solvent-exposed parts, which are broadened the most and often disappear from the observed spectrum around 200Â*K. Below the freezing of the bulk water,...
nmrlearner Journal club 0 02-05-2017 05:45 AM
[NMR paper] Statistical removal of background signals from high-throughput (1)H NMR line-broadening ligand-affinity screens.
Statistical removal of background signals from high-throughput (1)H NMR line-broadening ligand-affinity screens. Statistical removal of background signals from high-throughput (1)H NMR line-broadening ligand-affinity screens. J Biomol NMR. 2015 Jul 9; Authors: Worley B, Sisco NJ, Powers R Abstract NMR ligand-affinity screens are vital to drug discovery, are routinely used to screen fragment-based libraries, and used to verify chemical leads from high-throughput assays and virtual screens. NMR ligand-affinity screens are...
nmrlearner Journal club 0 07-12-2015 07:12 AM
Statistical removal of background signals from high-throughput 1 H NMR line-broadening ligand-affinity screens
Statistical removal of background signals from high-throughput 1 H NMR line-broadening ligand-affinity screens Abstract NMR ligand-affinity screens are vital to drug discovery, are routinely used to screen fragment-based libraries, and used to verify chemical leads from high-throughput assays and virtual screens. NMR ligand-affinity screens are also a highly informative first step towards identifying functional epitopes of unknown proteins, as well as elucidating the biochemical functions of proteinâ??ligand interaction at their binding interfaces....
nmrlearner Journal club 0 07-08-2015 11:11 PM
[U. of Ottawa NMR Facility Blog] Exponential Line Broadening - Video Tutorial
Exponential Line Broadening - Video Tutorial Exponential line broadening is an important NMR data processing tool. It involves multiplying the time domain signal by a decaying exponential function prior to Fourier transforming the data into the frequency domain. It is used to improve the signal-to-noise ratio and is more fully described in a previous post. The following short tutorial video demonstrates its use. http://4.bp.blogspot.com/-CozKHXyqcTA/UUdrJzrbyqI/AAAAAAAABG8/0FLtL9-4af0/s400/lb_vid.jpg
nmrlearner News from NMR blogs 0 03-19-2013 12:58 AM
Preparation of RNA samples with narrow line widths for solid state NMR investigations
Preparation of RNA samples with narrow line widths for solid state NMR investigations Publication year: 2012 Source:Journal of Magnetic Resonance</br> Wei Huang, Michael F. Bardaro, Gabriele Varani, Gary P. Drobny</br> Solid state NMR can provide detailed structural and dynamic information on biological systems that cannot be studied under solution conditions, and can investigate motions which occur with rates that cannot be fully studied by solution NMR. This approach has successfully been used to study proteins, but the application of multidimensional solid state...
nmrlearner Journal club 0 08-10-2012 08:40 PM
[Question from NMRWiki Q&A forum] residue information in case of line broadening (intensity drop ) of HSQC titration
residue information in case of line broadening (intensity drop ) of HSQC titration Dear Friends we have done HSQC gradient titration with targeted proteins , most of cross peaks we observed intensity drop , 30 out of 95 peaks ( 70 percent intensity drop of each cross peak ) , other cross peaks also we observe intensity drop less than 70 percent , we did n"t observe any chemical shift change .( May be it is due to intermediate exchange regime of complex ) .ITC experiment showing 12uM binding constant .AUC experiment result is complex size 33 kd . is their any method to extract...
nmrlearner News from other NMR forums 0 05-11-2012 10:36 AM
[Question from NMRWiki Q&A forum] How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ? Dear Friends we have done HSQC gradient titration with targeted proteins , most of cross peaks we observed intensity drop , 30 out of 95 peaks ( 70 percent intensity drop of each cross peak ) , other cross peaks also we observe intensity drop less than 70 percent , we did n"t observe any chemical shift change .( May be it is due to intermediate exchange regime of complex ) .ITC experiment showing 12uM binding constant .AUC experiment result is...
nmrlearner News from other NMR forums 0 05-09-2012 07:38 PM
[Question from NMRWiki Q&A forum] Line broadening in nmr
Line broadening in nmr Hello can some body help me in understanding the line broadening effect in NMR? I am working with protein and small molecules and I observed severe broadening at a protein to ligand ratio 1:20. I am pretty sure that its not aggregation since i have the free ligand spectrum without the protein which didnt showed any broadening effect. Hope somebody will guide me.. Check if somebody has answered this question on NMRWiki QA forum
nmrlearner News from other NMR forums 0 10-04-2011 08:47 PM



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 11:07 PM.


Map