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 04-25-2024, 04:20 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 NMR methods to detect fluoride binding and transport by membrane proteins

NMR methods to detect fluoride binding and transport by membrane proteins

Solid-state nuclear magnetic resonance (NMR) methods can probe the motions of membrane proteins in liposomes at the atomic level, and propel the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. High-resolution crystallography snapshots have provided a structural basis for fluoride channels. NMR is a powerful tool to build upon these snapshots and depict a dynamic picture of fluoride channels in native-like lipid bilayers. In this...

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding.
Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.nature.com-images-npg_logo.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines...
nmrlearner Journal club 0 10-08-2020 06:02 PM
[NMR paper] A Single Atom Change Facilitates the Membrane Transport of Green Fluorescent Proteins in Mammalian Cells
A Single Atom Change Facilitates the Membrane Transport of Green Fluorescent Proteins in Mammalian Cells Angewandte Chemie International Edition, EarlyView. More...
nmrlearner Journal club 0 05-09-2019 05:55 AM
[NMR paper] Solid-state NMR methods for oriented membrane proteins.
Solid-state NMR methods for oriented membrane proteins. Related Articles Solid-state NMR methods for oriented membrane proteins. Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:48-85 Authors: Hansen SK, Bertelsen K, Paaske B, Nielsen NC, Vosegaard T Abstract Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix...
nmrlearner Journal club 0 08-19-2015 03:24 PM
Solid-State NMR Methods for Oriented Membrane Proteins
Solid-State NMR Methods for Oriented Membrane Proteins Publication date: Available online 19 May 2015 Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br> Author(s): Sara K. Hansen , Kresten Bertelsen , Berit Paaske , Niels Chr. Nielsen , Thomas Vosegaard</br> Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix bundle membrane...
nmrlearner Journal club 0 05-19-2015 09:10 AM
[NMR paper] Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods. Related Articles Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods. Anal Biochem. 2013 Dec 9; Authors: Sahu D, Bastidas M, Showalter S Abstract There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs...
nmrlearner Journal club 0 12-18-2013 04:00 PM
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods Publication date: Available online 10 December 2013 Source:Analytical Biochemistry</br> Author(s): Debashish Sahu , Monique Bastidas , Scott Showalter</br> There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs by NMR spectroscopy is limited by the poor 1H-amide chemical shift dispersion...
nmrlearner Journal club 0 12-10-2013 04:48 AM
Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems
From The DNP-NMR Blog: Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems Cheng, C.Y. and S. Han, Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems. Annu Rev Phys Chem, 2013. 64(1): p. 507-32. http://www.ncbi.nlm.nih.gov/pubmed/23331309
nmrlearner News from NMR blogs 0 07-08-2013 02:17 PM
[NMR paper] Weak substrate binding to transport proteins studied by NMR.
Weak substrate binding to transport proteins studied by NMR. Related Articles Weak substrate binding to transport proteins studied by NMR. Biophys J. 1998 Dec;75(6):2794-800 Authors: Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible...
nmrlearner Journal club 0 11-17-2010 11:15 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 02:49 AM.


Map