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 07-12-2011, 08:16 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,173
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 Systematic Study of Protein Detection Mechanism of Self-Assembling 19F NMR/MRI Nanoprobes toward Rational Design and Improved Sensitivity

Systematic Study of Protein Detection Mechanism of Self-Assembling 19F NMR/MRI Nanoprobes toward Rational Design and Improved Sensitivity

Yousuke Takaoka, Keishi Kiminami, Keigo Mizusawa, Kazuya Matsuo, Michiko Narazaki, Tetsuya Matsuda and Itaru Hamachi



Journal of the American Chemical Society
DOI: 10.1021/ja203996c




Source: Journal of the American Chemical Society
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif Journal of the American Chemical Society DOI: 10.1021/ja2081185 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
nmrlearner Journal club 0 10-22-2011 10:16 AM
[NMR paper] Solution NMR study of DNA recognition mechanism of IRF4 protein.
Solution NMR study of DNA recognition mechanism of IRF4 protein. Related Articles Solution NMR study of DNA recognition mechanism of IRF4 protein. Nucleic Acids Symp Ser (Oxf). 2004;(48):105-6 Authors: Ishizaki I, Nomura M, Yamamoto K, Matsuyama T, Mishima M, Kojima C Transcription factor IRF-4 prefers the DNA sequence including CCGAAA. The consensus sequence of the IRF family proteins is NNGAAA, and all crystal structures indicate the NN region does not interact with IRF proteins directly. Here the sequence preference of IRF-4 was...
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] Design of small volume HX and triple-resonance probes for improved limits of detectio
Design of small volume HX and triple-resonance probes for improved limits of detection in protein NMR experiments. Related Articles Design of small volume HX and triple-resonance probes for improved limits of detection in protein NMR experiments. J Magn Reson. 2003 Sep;164(1):128-35 Authors: Li Y, Logan TM, Edison AS, Webb A Three- and four-frequency nuclear magnetic-resonance probes have been designed for the study of small amounts of protein. Both "HX" (1H, X, and 2H channels) and "triple-resonance" (1H, 15N, 13C, and 2H) probes were...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection.
Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection. Related Articles Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection. J Magn Reson. 2001 May;150(1):43-8 Authors: Hong M, Yamaguchi S A method for enhancing the sensitivity of 15N spectra of nonspinning solids through 1H indirect detection is introduced. By sampling the 1H signals in the windows of a pulsed spin-lock sequence, high-sensitivity 1H spectra can be obtained in two-dimensional (2D) spectra whose indirect dimension yields the 15N chemical...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the ap
Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment. Related Articles Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment. J Biomol NMR. 2001 Mar;19(3):231-41 Authors: Iwahara J, Wojciak JM, Clubb RT The NMR spectra of the complex between the DNA-binding domain of the Dead ringer protein (DRI-DBD, Gly262-Gly398) and its DNA binding site...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] A systematic case study on using NMR models for molecular replacement: p53 tetrameriz
A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisited. Related Articles A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisited. Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1535-40 Authors: Chen YW, Clore GM Molecular replacement using search models derived from nuclear magnetic resonance (NMR) spectroscopy has often proved problematic. It has been known for some time that the overall differences in atomic positions (r.m.s.d.)...
nmrlearner Journal club 0 11-19-2010 08:29 PM
Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low c
Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low concentration of protein. Related Articles Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low concentration of protein. Magn Reson Chem. 2010 Oct 18; Authors: Xia Y, Zhu Q, Jun KY, Wang J, Gao X Saturation transfer difference (STD)-NMR has been widely used to screen ligand compound libraries for their binding activities to proteins and to determine the binding epitopes of the ligands. We report herein, a Clean STD-NMR method...
nmrlearner Journal club 0 10-22-2010 06:02 AM
[NMR paper] High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substra
High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein. Nucleic Acids Res. 1996 Feb 15;24(4):611-8...
nmrlearner Journal club 0 08-22-2010 02:27 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 01:51 AM.


Map