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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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  
Old 02-29-2024, 10:00 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 Interactions between the protein barnase and co-solutes studied by NMR

Interactions between the protein barnase and co-solutes studied by NMR

Protein solubility and stability depend on the co-solutes present. There is little theoretical basis for selection of suitable co-solutes. Some guidance is provided by the Hofmeister series, an empirical ordering of anions according to their effect on solubility and stability; and by osmolytes, which are small organic molecules produced by cells to allow them to function in stressful environments. Here, NMR titrations of the protein barnase with Hofmeister anions and osmolytes are used to...

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Interactions between the protein barnase and co-solutes studied by NMR | Communications Chemistry - Nature.com
Interactions between the protein barnase and co-solutes studied by NMR | Communications Chemistry - Nature.com Interactions between the protein barnase and co-solutes studied by NMR | Communications Chemistry Nature.com Read here
nmrlearner Online News 0 02-28-2024 09:53 PM
[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry. Related Articles Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry. J Biol Chem. 2014 Aug 13; Authors: Meneses E, Mittermaier A Abstract Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
nmrlearner Journal club 0 08-15-2014 12:53 PM
[NMR paper] Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design. Related Articles Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design. Curr Protein Pept Sci. 2012 Dec 10; Authors: Fernandez-Alonso MD, Diaz D, Berbis MA, Marcelo F, Jimenez-Barbero J Abstract Diseases that result from infection are, in general, a consequence of specific interactions between a pathogenic organism and the cells. The study of host-pathogen interactions has provided insights for the design of...
nmrlearner Journal club 0 02-03-2013 10:22 AM
[NMR paper] Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy wit
Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents. Related Articles Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents. Chembiochem. 2004 Apr 2;5(4):467-73 Authors: Hilty C, Wider G, Fernández C, Wüthrich K For solution NMR studies of the structure and function of membrane proteins, these macromolecules have to be reconstituted and solubilized in detergent micelles. Detailed characterization of the mixed...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dy
Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR. Related Articles Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR. Eur J Biochem. 2003 Dec;270(23):4606-14 Authors: Lamosa P, Turner DL, Ventura R, Maycock C, Santos H Heteronuclear NMR relaxation measurements and hydrogen exchange data have been used to characterize protein dynamics in the presence or absence of...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin. Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin. Biochemistry. 2003 Jun 17;42(23):7068-76 Authors: Worrall JA, Reinle W, Bernhardt R, Ubbink M The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitut
Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitution of the enzyme with 13C- and 15N-labelled flavin. Related Articles Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitution of the enzyme with 13C- and 15N-labelled flavin. Eur J Biochem. 2000 Aug;267(16):5156-67 Authors: Fleischmann G, Lederer F, Müller F, Bacher A, Rüterjans H A new procedure was devised for reversibly removing the flavin from flavocytochrome b2. It allowed reconstitution with selectively enriched 13C- and...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] A mini-protein designed by removing a module from barnase: molecular modeling and NMR
A mini-protein designed by removing a module from barnase: molecular modeling and NMR measurements of the conformation. Related Articles A mini-protein designed by removing a module from barnase: molecular modeling and NMR measurements of the conformation. Protein Eng. 1999 Aug;12(8):673-80 Authors: Takahashi K, Noguti T, Hojo H, Yamauchi K, Kinoshita M, Aimoto S, Ohkubo T, G? M A globular domain can be decomposed into compact modules consisting of contiguous 10-30 amino acid residues. The correlation between modules and exons observed in...
nmrlearner Journal club 0 11-18-2010 08:31 PM



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 01:57 AM.


Map