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 01-22-2011, 01:52 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 Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.

Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.

Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.

Magn Reson Chem. 2011 Feb;49(2):65-9

Authors: Middleton DA

Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary structure, alignment and registration of ?-strands within amyloid fibrils and identify the tertiary and quaternary contacts defining the packing of the ?-sheet layers. Detection of (14) N?(13) C dipolar couplings may provide potentially useful additional structural constraints on ?-sheet packing within amyloid fibrils but has not until now been exploited for this purpose. Here a frequency-selective, transfer of population in double resonance SSNMR experiment is used to detect a weak (14) N?(13) C dipolar coupling in amyloid-like fibrils of the peptide H(2) N-SNNFGAILSS-COOH, which was uniformly (13) C and (15) N labelled across the four C-terminal amino acids. The (14) N?(13) C interatomic distance between leucine and asparagine side groups is constrained between 2.4 and 3.8 Å, which allows current structural models of the ?-spine arrangement within the fibrils to be refined. This procedure could be useful for the general structural analysis of other proteins in condensed phases and environments, such as biological membranes. Copyright © 2011 John Wiley & Sons, Ltd.

PMID: 21254226 [PubMed - in process]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion. Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion. Angew Chem Int Ed Engl. 2011 Sep 16; Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M PMID: 21928443
nmrlearner Journal club 0 09-20-2011 03:10 PM
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion. Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion. Angew Chem Int Ed Engl. 2011 Sep 14; Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M PMID: 21915969
nmrlearner Journal club 0 09-15-2011 08:31 PM
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR. Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR. J Magn Reson. 2011 Mar 21; Authors: Schanda P, Meier BH, Ernst M The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling...
nmrlearner Journal club 0 04-13-2011 11:57 PM
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 21 March 2011</br> Paul, Schanda , Beat H., Meier , Matthias, Ernst</br> The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in...
nmrlearner Journal club 0 03-22-2011 07:30 AM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure. Solid-State NMR Studies of Amyloid Fibril Structure. Annu Rev Phys Chem. 2010 Apr 2; Authors: Tycko R Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
nmrlearner Journal club 0 01-12-2011 11:11 AM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture. Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture. Magn Reson Chem. 2011 Jan 3; Authors: Middleton DA Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
nmrlearner Journal club 0 01-05-2011 09:51 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy. Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy. J Am Chem Soc. 2010 Dec 27; Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
nmrlearner Journal club 0 12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif Journal of the American Chemical Society DOI: 10.1021/ja107847d http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/iFwgRBt-zto
nmrlearner Journal club 0 12-28-2010 05:27 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 11:15 AM.


Map