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 05-04-2019, 01:24 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,327
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 Positively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.

Positively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.

Related Articles Positively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.

J Phys Chem B. 2019 May 01;:

Authors: Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C

Abstract
Proteins are often tagged for visualization or delivery in the "sea" of other macromolecules in cells but how tags affect protein mobility remains poorly understood. Here, we employ 19F in-cell NMR to quantify the mobility of proteins with charged tags in Escherichia coli cells and Xenopus laevis oocytes. We find that the transient charge-charge interactions between the tag and cellular components affect protein mobility. More specifically, positively-charged tags impede protein mobility.


PMID: 31042382 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy.
Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy. Anal Bioanal Chem. 2017 Nov 28;: Authors: Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C Abstract Protein diffusion in living cells might differ significantly from that measured in vitro. Little is known...
nmrlearner Journal club 0 12-01-2017 09:24 PM
A Soluble, Folded Protein without Charged Amino AcidResidues
A Soluble, Folded Protein without Charged Amino AcidResidues http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00269/20160628/images/medium/bi-2016-00269x_0007.gif Biochemistry DOI: 10.1021/acs.biochem.6b00269 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/Gkdzui0Df1I More...
nmrlearner Journal club 0 07-07-2016 04:21 AM
[NMR paper] A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR. A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR. J Am Chem Soc. 2015 Sep 8; Authors: Thiagarajan-Rosenkranz Paltr Uic Edu P, Draney AW, Smrt ST, Lorieau JL Abstract Residual Dipolar Couplings (RDCs) are integral to the refinement of membrane protein structures by NMR since they accurately define the orientation of helices and other structural...
nmrlearner Journal club 0 09-09-2015 11:49 AM
[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
NMR spectroscopy of proteins encapsulated in a positively charged surfactant. Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant. J Magn Reson. 2005 Jul;175(1):158-62 Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide
NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide. Related Articles NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide. Biochim Biophys Acta. 1998 Nov 8;1442(2-3):137-47 Authors: van Lieshout E, Hemminga MA To obtain a better understanding of the electrostatic nature of protein-nucleic acid interactions, we have investigated the interaction of a double-stranded decamer d(GGAAATTTCC)2 with a synthetic arginine and lysine-rich pentacosapeptide (Pep25), using NMR and optical...
nmrlearner Journal club 0 11-17-2010 11:15 PM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector Abstract The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To address these problems, a modified cold-shock expression system containing a glutathione S-transferase (GST) tag, the pCold-GST system, was investigated. The pCold-GST system successfully expressed 9 out of 10 proteins...
nmrlearner Journal club 0 09-18-2010 04:53 AM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine. Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine. Biochemistry. 1994 Jan 25;33(3):644-50 Authors: Fraenkel Y, Gershoni JM, Navon G A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine. Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine. Biochemistry. 1994 Jan 25;33(3):644-50 Authors: Fraenkel Y, Gershoni JM, Navon G A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
nmrlearner Journal club 0 08-22-2010 03:33 AM


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 11:44 AM.


Map