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 Rating: Thread Rating: 1 votes, 5.00 average. Display Modes
  #1  
Unread 12-01-2010, 06:56 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 21,495
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 Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Related Articles Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Protein Sci. 2005 Nov;14(11):2919-21

Authors: Peterson RW, Pometun MS, Shi Z, Wand AJ

NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids is emerging as a tool for biophysical studies of proteins in atomic detail in a variety of otherwise inaccessible contexts. The central element of the approach is the encapsulation of the protein of interest within the aqueous core of a reverse micelle with high structural fidelity. The process of encapsulation is highly dependent upon the nature of the surfactant(s) employed. Here we describe novel mixtures of surfactants that are capable of successfully encapsulating a range of types of proteins under a variety of conditions.

PMID: 16199658 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids Abstract Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods, such as TROSY in conjunction with isotopic labeling schemes that are often expensive and generally reduce the potential information available. We have developed the reverse micelle encapsulation strategy as an alternative approach. Encapsulation of...
nmrlearner Journal club 0 07-15-2011 09:10 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. J Biomol NMR. 2011 Jul 12; Authors: Nucci NV, Marques BS, Bédard S, Dogan J, Gledhill JM, Moorman VR, Peterson RW, Valentine KG, Wand AL, Wand AJ Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30*kDa require complex...
nmrlearner Journal club 0 07-13-2011 06:42 PM
[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] Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolve
Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. Related Articles Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. J Biomol NMR. 2003 Apr;25(4):313-23 Authors: Babu CR, Flynn PF, Wand AJ Encapsulating a protein in a reverse micelle and dissolving it in a low-viscosity solvent can lower the rotational correlation time of a protein and thereby provides a novel strategy for studying proteins in a variety of contexts. The...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] A simple and effective NMR cell for studies of encapsulated proteins dissolved in low
A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents. Related Articles A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents. J Biomol NMR. 2002 Aug;23(4):311-6 Authors: Flynn PF, Milton MJ, Babu CR, Wand AJ Application of triple-resonance and isotope-edited-NOE methods to the study of increasingly larger macromolecules and their complexes remains a central goal of solution NMR spectroscopy. The slow reorientational motion of larger molecules...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Related Articles High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15299-302 Authors: Wand AJ, Ehrhardt MR, Flynn PF The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] What NMR can tell us about where lung surfactant proteins live.
What NMR can tell us about where lung surfactant proteins live. Related Articles What NMR can tell us about where lung surfactant proteins live. Biochem Soc Trans. 1997 Aug;25(3):1103-7 Authors: Morrow MR, Taneva S, Dico AS, Hancock J, Keough KM 2H-NMR is beginning to provide some insights into the way in which the hydrophobic surfactant proteins SP-B and SP-C interact with phospholipid bilayers in multilamellar structures. Both proteins have a significant effect on slow bilayer motions. In many ways, the effect of SP-C on the surrounding...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of h
Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of homonuclear two-dimensional J-resolved spectroscopy to urine and blood plasma for spectral simplification and assignment. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of homonuclear two-dimensional J-resolved spectroscopy to urine and blood plasma for spectral simplification and assignment. J Pharm Biomed Anal. 1993...
nmrlearner Journal club 0 08-21-2010 11:53 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 05:14 AM.


Map