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 07-11-2017, 09:20 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 22,204
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 Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation

Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation

Publication date: Available online 10 July 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy

Author(s): Nicola Salvi, Anton Abyzov, Martin Blackledge

Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behavior of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for understanding fundamental biological processes, the molecular basis of their activity still remains largely unknown. The functional mechanisms exploited by IDPs in their interactions with other biomolecules are defined by their intrinsic dynamic modes and associated timescales, justifying the considerable interest over recent years in the development of technologies adapted to measure and describe this behavior. NMR spin relaxation delivers information-rich, site-specific data reporting on conformational fluctuations occurring throughout the molecule. Here we review recent progress in the use of 15N relaxation to identify local backbone dynamics and long-range chain-like motions in unfolded proteins.
Graphical abstract








More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation. Related Articles Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation. J Phys Chem Lett. 2016 Jun 14; Authors: Salvi N, Abyzov A, Blackledge M Abstract Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their functional states. Although this plasticity is essential to their function, little is known about the dynamics underlying...
nmrlearner Journal club 0 06-15-2016 11:12 PM
[NMR paper] Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy. Related Articles Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy. Biochim Biophys Acta. 2016 Jun 8; Authors: Yao S, Lee EF, Pettikiriarachchi A, Evangelista M, Keizer DW, Fairlie WD Abstract Beclin 1 is a 450 amino acid protein that plays critical roles in the early stages of autophagosome...
nmrlearner Journal club 0 06-12-2016 03:35 PM
[NMR paper] Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy.
Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy. Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy. Chem Rev. 2014 Apr 11; Authors: Jensen MR, Zweckstetter M, Huang JR, Blackledge M PMID: 24725176
nmrlearner Journal club 0 04-15-2014 10:38 AM
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.
Toward optimal-resolution NMR of intrinsically disordered proteins. Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins. J Magn Reson. 2014 Apr;241:41-52 Authors: Nová?ek J, Zídek L, Sklená? V Abstract Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their...
nmrlearner Journal club 0 03-25-2014 11:49 AM
Toward optimal-resolution NMR of intrinsically disordered proteins
Toward optimal-resolution NMR of intrinsically disordered proteins Publication date: April 2014 Source:Journal of Magnetic Resonance, Volume 241</br> Author(s): Ji?í Nová?ek , Lukáš Žídek , Vladimír Sklená?</br> Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular...
nmrlearner Journal club 0 03-21-2014 12:52 AM
[NMR paper] Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering.
Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering. Related Articles Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering. Structure. 2013 Dec 18; Authors: Schwalbe M, Ozenne V, Bibow S, Jaremko M, Jaremko L, Gajda M, Jensen MR, Biernat J, Becker S, Mandelkow E, Zweckstetter M, Blackledge M Abstract The development of molecular descriptions of intrinsically...
nmrlearner Journal club 0 12-24-2013 01:04 PM
[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR.
Describing intrinsically disordered proteins at atomic resolution by NMR. Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR. Curr Opin Struct Biol. 2013 Mar 29; Authors: Jensen MR, Ruigrok RW, Blackledge M Abstract There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...
nmrlearner Journal club 0 04-03-2013 08:22 PM
Describing intrinsically disordered proteins at atomic resolution by NMR
Describing intrinsically disordered proteins at atomic resolution by NMR Available online 29 March 2013 Publication year: 2013 Source:Current Opinion in Structural Biology</br> </br> There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...
nmrlearner Journal club 0 03-29-2013 07:52 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 - 2022, 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 02:18 AM.


Map