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 02-02-2022, 04:56 PM
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 Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca2+-ligated calmodulin [Chemistry]

Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca2+-ligated calmodulin [Chemistry]

Thomas Schmidt, Jaekyun Jeon, Wai-Ming Yau, Charles D. Schwieters, Robert Tycko, G. Marius Clore...
Date: 2022-02-01

Recent advances in rapid mixing and freeze quenching have opened the path for time-resolved electron paramagnetic resonance (EPR)-based double electron-electron resonance (DEER) and solid-state NMR of protein–substrate interactions. DEER, in conjunction with phase memory time filtering to quantitatively extract species populations, permits monitoring time-dependent probability distance distributions between pairs of... Read More


PNAS:
Number: 6
Volume: 119
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR.
Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR. Related Articles Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR. ACS Biomater Sci Eng. 2016 May 09;2(5):758-767 Authors: Callone E, Dirč S, Hu X, Motta A Abstract This study is devoted to the deep evaluation of processing-induced protein conformation changes by using silk fibroin fibers and their cast films stabilized by different...
nmrlearner Journal club 0 01-15-2021 04:25 PM
[ASAP] Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase Jaekyun Jeon, Wai-Ming Yau, and Robert Tycko https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c11156/20201207/images/medium/ja0c11156_0007.gif Journal of the American Chemical Society DOI: 10.1021/jacs.0c11156 http://feeds.feedburner.com/~r/acs/jacsat/~4/pGPDzdJltQs
nmrlearner Journal club 0 12-08-2020 01:36 PM
[NMR paper] Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase. Related Articles Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase. J Am Chem Soc. 2020 Dec 07;: Authors: Jeon J, Yau WM, Tycko R Abstract Calmodulin (CaM) mediates a wide range of biological responses to changes in...
nmrlearner Journal club 0 12-08-2020 01:36 PM
[ASAP] Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex
Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01073/20200216/images/medium/bi9b01073_0004.gif Biochemistry DOI: 10.1021/acs.biochem.9b01073 http://feeds.feedburner.com/~r/acs/bichaw/~4/9uJdixEmET4 More...
nmrlearner Journal club 0 02-29-2020 09:52 PM
[NMR paper] Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations. Related Articles Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations. Solid State Nucl Magn Reson. 2017 Mar 18;: Authors: Medeiros-Silva J, Jekhmane S, Baldus M, Weingarth M Abstract (1)H-detected solid-state NMR in combination with (1)H/(2)D exchange steps allows for the direct identification of very strong hydrogen bonds in membrane proteins....
nmrlearner Journal club 0 03-28-2017 03:06 PM
Hydrogen bond strength in membrane proteins by time-resolved 1H-detected solid-state NMR and MD simulations
Hydrogen bond strength in membrane proteins by time-resolved 1H-detected solid-state NMR and MD simulations Publication date: Available online 18 March 2017 Source:Solid State Nuclear Magnetic Resonance</br> Author(s): Joćo Medeiros-Silva, Shehrazade Jekhmane, Marc Baldus, Markus Weingarth</br> 1H-detected solid-state NMR in combination with 1H/2D exchange steps allows for the direct identification of very strong hydrogen bonds in membrane proteins. On the example of the membrane-embedded potassium channel KcsA, we quantify the longevity of such very strong...
nmrlearner Journal club 0 03-19-2017 07:03 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
nmrlearner Journal club 0 01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. J Biomol NMR. 2011 Jan 21; Authors: Etzkorn M, Böckmann A, Baldus M It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
nmrlearner Journal club 0 01-22-2011 01:52 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 10:16 AM.


Map