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 02-21-2015, 11:48 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
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 Site-SpecificProtonation Kinetics of Acidic SideChains in Proteins Determined by pH-Dependent Carboxyl 13C NMR Relaxation

Site-SpecificProtonation Kinetics of Acidic SideChains in Proteins Determined by pH-Dependent Carboxyl 13C NMR Relaxation

Johan Wallerstein, Ulrich Weininger, M. Ashhar I. Khan, Sara Linse and Mikael Akke



Journal of the American Chemical Society
DOI: 10.1021/ja513205s




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
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs) Publication date: Available online 12 February 2015 Source:Journal of Magnetic Resonance</br> Author(s): Tomáš Hošek , Sergi Gil-Caballero , Roberta Pierattelli , Bernhard Brutscher , Isabella C. Felli</br> Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%)...
nmrlearner Journal club 0 02-12-2015 07:48 PM
[NMR paper] Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation.
Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation. Related Articles Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation. J Am Chem Soc. 2015 Feb 10; Authors: Wallerstein J, Weininger U, Khan MA, Linse S, Akke M Abstract Proton transfer dynamics plays a critical role in many biochemical processes, such as proton pumping across membranes and enzyme catalysis. The large majority of enzymes...
nmrlearner Journal club 0 02-11-2015 04:19 PM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation. Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation. J Magn Reson. 2014 Sep 20;248C:8-12 Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K Abstract (15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms...
nmrlearner Journal club 0 10-06-2014 12:37 PM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation
Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation Publication date: Available online 20 September 2014 Source:Journal of Magnetic Resonance</br> Author(s): Alexey Krushelnitsky , Tatiana Zinkevich , Bernd Reif , Kay Saalwächter</br> 15N NMR relaxation rate R 1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s - ms timescale range. On the basis of a comparison of 2D site-resolved with 1D integrated 15N...
nmrlearner Journal club 0 09-20-2014 07:51 PM
[NMR paper] Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD
Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD simulations. Related Articles Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD simulations. Biochemistry. 2003 Dec 2;42(47):13856-68 Authors: Hu H, Clarkson MW, Hermans J, Lee AL To gain physical insights into how proteins respond to changes in pH, the picosecond to nanosecond time scale dynamics of the small serine protease inhibitor eglin c have been studied by NMR spin relaxation experiments and MD simulations under two...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor. Related Articles 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor. J Biol Chem. 2000 Dec 15;275(50):39444-50 Authors: Chi Y, Kumar TK, Chiu IM, Yu C 15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] Involvement of various amino- and carboxyl-terminal residues in the active site of th
Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins. Related Articles Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy:
Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein. Related Articles Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein. Biochemistry. 1990 Jul 3;29(26):6303-13 Authors: Henry GD, Sykes BD The coat protein of the filamentous coliphage M13 is a 50-residue polypeptide which spans the...
nmrlearner Journal club 0 08-21-2010 11:04 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 04:30 PM.


Map