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 04-10-2018, 12:43 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 19,906
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 Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.

Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.

Related Articles Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.

J Phys Chem Lett. 2018 Mar 15;9(6):1307-1311

Authors: Vasa SK, Singh H, Rovó P, Linser R

Abstract
Solid-state NMR has been employed for characterization of a broad range of biomacromolecules and supramolecular assemblies. However, because of limitations in sensitivity and resolution, the size of the individual monomeric units has rarely exceeded 15 kDa. As such, enzymes, which are often more complex and comprise long peptide chains, have not been easily accessible, even though manifold desirable information could potentially be provided by solid-state NMR studies. Here, we demonstrate that more than 1200 backbone and side-chain chemical shifts can be reliably assessed from minimal sample quantities for a 29 kDa human enzyme of the carbonic anhydrase family, giving access to its backbone dynamics and intermolecular interactions with a small-molecule inhibitor. The possibility of comprehensive assessment of enzymes in this molecular-weight regime without molecular-tumbling-derived limitations enables the study of residue-specific properties important for their mode of action as well as for pharmacological interference in this and many other enzymes.


PMID: 29481091 [PubMed - indexed for MEDLINE]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Dynamics of Membrane Proteins Studied by Solid State 2H NMR Relaxation
Dynamics of Membrane Proteins Studied by Solid State 2H NMR Relaxation Publication date: 2 February 2018 Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br> Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown</br> </br></br> </br></br> More...
nmrlearner Journal club 0 02-07-2018 03:41 PM
[NMR paper] Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy. Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy. Angew Chem Weinheim Bergstr Ger. 2015 Dec 14;127(51):15594-15598 Authors: Lamley JM, Öster C, Stevens RA, Lewandowski JR Abstract Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the...
nmrlearner Journal club 0 08-03-2016 04:58 AM
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation Publication date: 16 February 2016 Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br> Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown</br> </br></br> </br></br> More...
nmrlearner Journal club 0 02-17-2016 07:50 PM
[NMR paper] Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy. Angew Chem Int Ed Engl. 2015 Nov 2; Authors: Lamley JM, Öster C, Stevens RA,...
nmrlearner Journal club 0 11-09-2015 02:00 AM
[NMR paper] Lipid dynamics studied by calculation of 31P solid-state NMR spectra using ensembles from molecular dynamics simulations.
Lipid dynamics studied by calculation of 31P solid-state NMR spectra using ensembles from molecular dynamics simulations. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Lipid dynamics studied by calculation of 31P solid-state NMR spectra using ensembles from molecular dynamics simulations. J Phys Chem B. 2014 May 15;118(19):5119-29 Authors: Hansen SK, Vestergaard M, Thøgersen L, Schiøtt B, Nielsen NC, Vosegaard T Abstract We present a method to...
nmrlearner Journal club 0 04-22-2015 03:33 PM
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2 Abstract The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the...
nmrlearner Journal club 0 11-17-2014 12:39 AM
[NMR paper] Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation. Related Articles Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation. J Biomol NMR. 2013 Sep 19; Authors: Zinkevich T, Chevelkov V, Reif B, Saalwächter K, Krushelnitsky A Abstract
nmrlearner Journal club 0 09-21-2013 06:50 PM
[NMR paper] Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spe
Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy. J Magn Reson. 1999 Jun;138(2):244-55 Authors: Krushelnitsky A, Reichert D, Hempel G, Fedotov V, Schneider H, Yagodina L, Schulga A Superslow backbone dynamics of the protein barstar and the polypeptide polyglycine was studied by...
nmrlearner Journal club 0 08-21-2010 04:03 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 12:35 PM.


Map