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  
Unread 06-02-2021, 05:10 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,188
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 (17)O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding

(17)O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding

Oxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (^(17)O), therefore, has been proposed as a useful probe that can provide detailed information about various physicochemical features of proteins. This is attributed to the facts that (1) ^(17)O is an active isotope for nuclear magnetic resonance (NMR) spectroscopic approaches; (2) NMR spectroscopy is one of the most suitable tools for...

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy.
Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy. Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy. Methods Mol Biol. 2018;1764:73-85 Authors: Ortega-Roldan JL, Blackledge M, Jensen MR Abstract In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the binding affinity from a quantitative analysis of the experimental data. In particular, we...
nmrlearner Journal club 0 04-02-2018 03:36 PM
Characterizing the Structure and Oligomerization ofMajor Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and ComplementaryBiophysical Tools
Characterizing the Structure and Oligomerization ofMajor Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and ComplementaryBiophysical Tools http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00020/20170307/images/medium/bi-2017-000207_0009.gif Biochemistry DOI: 10.1021/acs.biochem.7b00020 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/Z1DtTF7H4jc More...
nmrlearner Journal club 0 03-08-2017 09:02 AM
[NMR paper] Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy. Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy. Methods Mol Biol. 2015;1229:325-33 Authors: Joseph PR, Poluri KM, Sepuru KM, Rajarathnam K Abstract Solution nuclear magnetic resonance (NMR) spectroscopy and, in particular, chemical shift perturbation (CSP) titration experiments are ideally suited for characterizing the binding interface of macromolecular complexes. (1)H-(15) N-HSQC-based CSP studies have...
nmrlearner Journal club 0 10-19-2014 01:27 PM
[NMR paper] Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction. Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction. Biomacromolecules. 2013 Sep 11; Authors: Sampath S, Jenkins JE, Butler E, Kim J, Henning RW, Holland GP, Yarger JL Abstract This study provides a detailed secondary structural characterization of major ampullate dragline silk from Latrodectus hesperus (black widow) spiders. X-ray diffraction results show...
nmrlearner Journal club 0 09-13-2013 12:05 PM
Co-Translational Protein Folding on the Ribosome: using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains
Co-Translational Protein Folding on the Ribosome: using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains 29 January 2013 Publication year: 2013 Source:Biophysical Journal, Volume 104, Issue 2, Supplement 1</br> </br> </br> </br></br>
nmrlearner Journal club 0 02-03-2013 10:13 AM
Development of 43Ca solid state NMR spectroscopy as a probe of local structure in inorganic and molecular materials
Development of 43Ca solid state NMR spectroscopy as a probe of local structure in inorganic and molecular materials Available online 17 May 2012 Publication year: 2012 Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br> </br> Graphical abstract
nmrlearner Journal club 0 12-01-2012 06:10 PM
Development of 43Ca NMR Solid State NMR Spectroscopy as a Probe of Local Structure in Inorganic and Molecular Materials
Development of 43Ca NMR Solid State NMR Spectroscopy as a Probe of Local Structure in Inorganic and Molecular Materials Publication year: 2012 Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br> Danielle Laurencin, Mark E. Smith</br> Graphical abstract http://origin-ars.els-cdn.com/content/image/1-s2.0-S0079656512000684-fx1.jpg Graphical abstract Highlights
nmrlearner Journal club 0 05-17-2012 11:37 PM
[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods. 2004 Sep;34(1):133-43 Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...
nmrlearner Journal club 0 11-24-2010 10:01 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 01:20 PM.


Map