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 10-28-2014, 02:42 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,045
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 Triple resonance-based 13 C α and 13 C β CEST experiments for studies of ms timescale dynamics in proteins

Triple resonance-based 13 C α and 13 C β CEST experiments for studies of ms timescale dynamics in proteins

Abstract

A pair of triple resonance based CEST pulse schemes are presented for measuring 13Cα and 13Cβ chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of 13Cα or 13Cβ spins of major (ground) and minor (excited) conformers are obtained in a pseudo 3rd dimension that is generated by quantifying modulations of cross peaks in 15N, 1HN correlation spectra. An application to the folding reaction of a G48A mutant of the Fyn SH3 domain is presented, illustrating and validating the methodology.



Source: Journal of Biomolecular NMR
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Time-shared experiments for efficient assignment of triple-selectively labeled proteins
Time-shared experiments for efficient assignment of triple-selectively labeled proteins Publication date: Available online 30 September 2014 Source:Journal of Magnetic Resonance</br> Author(s): Frank Lhr , Aisha Laguerre , Christoph Bock , Sina Reckel , Peter J. Connolly , Norzehan Abdul-Manan , Franz Tumulka , Rupert Abele , Jonathan M. Moore , Volker Dtsch</br> Combinatorial triple-selective labeling facilitates the NMR assignment process for proteins that are subject to signal overlap and insufficient signal-to-noise in standard triple-resonance...
nmrlearner Journal club 0 10-01-2014 02:48 AM
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins Publication date: Available online 4 March 2014 Source:Journal of Magnetic Resonance</br> Author(s): Veniamin Chevelkov , Birgit Habenstein , Antoine Loquet , Karin Giller , Stefan Becker , Adam Lange</br> Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained...
nmrlearner Journal club 0 03-04-2014 06:37 PM
[NMR paper] Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry. Related Articles Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry. J Am Chem Soc. 2013 Nov 14; Authors: Charlier CD, Khan SN, Marquardsen T, Pelupessy P, Reiss V, Sakellariou D, Bodenhausen G, Engelke F, Ferrage F Abstract Understanding the molecular determinants underlying protein function requires the characterization of both structure and dynamics at atomic resolution. Nuclear relaxation rates allow a precise...
nmrlearner Journal club 0 11-16-2013 03:14 PM
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins Publication year: 2011 Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 423-441</br> Lewis E.*Kay, Mitsuhiko*Ikura, Rolf*Tschudin, Ad*Bax</br> Four new and complementary three-dimensional triple-resonance experiments are described for obtaining complete backboneH,C, andN resonance assignments of proteins uniformly enriched withC andN. The new methods all rely onH detection and use multiple magnetization transfers through well-resolved one-bondJcouplings. Therefore, the...
nmrlearner Journal club 0 12-11-2011 07:57 AM
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins Abstract Extensive resonance overlap exacerbates assignment of intrinsically disordered proteins (IDPs). This issue can be circumvented by utilizing 15N, 13C? and 1HN spins, where the chemical shift dispersion is mainly dictated by the characteristics of consecutive amino acid residues. Especially 15N and 13C? spins offer superior chemical shift dispersion in comparison to 13Cα and 13Cβ spins. However, HN-detected experiments...
nmrlearner Journal club 0 01-29-2011 05:31 AM
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15N??1HN cross peaks. For such residues, one cannot unambiguously link the ??left?? side of the NH root to the ??right?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...
nmrlearner Journal club 0 12-31-2010 08:38 PM
[NMR paper] Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR
Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments. Related Articles Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments. Protein Sci. 2005 Mar;14(3):735-42 Authors: Massi F, Grey MJ, Palmer AG NMR spin relaxation experiments are used to characterize the dynamics of the backbone of ubiquitin. Chemical exchange processes affecting residues Ile 23, Asn 25, Thr 55, and Val 70 are characterized using on- and off-resonance...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Protein dynamics measurements by TROSY-based NMR experiments.
Protein dynamics measurements by TROSY-based NMR experiments. Related Articles Protein dynamics measurements by TROSY-based NMR experiments. J Magn Reson. 2000 Apr;143(2):423-6 Authors: Zhu G, Xia Y, Nicholson LK, Sze KH The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T(1), T(2), and NOE of backbone (15)N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT...
nmrlearner Journal club 0 11-18-2010 09:15 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 - 2020, 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 11:57 AM.


Map