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 03-16-2017, 06:36 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,733
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 Genotype evaluation of cowpea seeds (Vigna unguiculata) using (1)H qNMR combined with exploratory tools and solid-state NMR.

Genotype evaluation of cowpea seeds (Vigna unguiculata) using (1)H qNMR combined with exploratory tools and solid-state NMR.

Related Articles Genotype evaluation of cowpea seeds (Vigna unguiculata) using (1)H qNMR combined with exploratory tools and solid-state NMR.

Food Res Int. 2017 Jan;91:140-147

Authors: Alves Filho EG, Silva LM, Teofilo EM, Larsen FH, de Brito ES

Abstract
The ultimate aim of this study was to apply a non-targeted chemometric analysis (principal component analysis and hierarchical clustering analysis using the heat map approach) of NMR data to investigate the variability of organic compounds in nine genotype cowpea seeds, without any complex pre-treatment. In general, both exploratory tools show that Tvu 233, CE-584, and Setentão genotypes presented higher amount mainly of raffinose and Tvu 382 presented the highest content of choline and least content of raffinose. The evaluation of the aromatic region showed the Setentão genotype with highest content of niacin/vitamin B3 whereas Tvu 382 with lowest amount. To investigate rigid and mobile components in the seeds cotyledon, (13)C CP and SP/MAS solid-state NMR experiments were performed. The cotyledon of the cowpea comprised a rigid part consisting of starch as well as a soft portion made of starch, fatty acids, and protein. The variable contact time experiment suggests the presence of lipid-amylose complexes.


PMID: 28290318 [PubMed - in process]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements. Related Articles Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements. Phys Chem Chem Phys. 2015 Aug 3; Authors: Lamley JM, Lougher MJ, Sass HJ, Rogowski M, Grzesiek S, Lewandowski JR Abstract Typically, protein dynamics involve a complex hierarchy of motions occurring on different time scales between conformations separated by a range...
nmrlearner Journal club 0 08-04-2015 03:00 PM
Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA
Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA Abstract The automated assignment of NOESY cross peaks has become a fundamental technique for NMR protein structure analysis. A widely used algorithm for this purpose is implemented in the program CYANA. It has been used for a large number of structure determinations of proteins in solution but a systematic evaluation of its performance has not yet been reported. In this paper we systematically analyze the reliability of combined automated NOESY assignment...
nmrlearner Journal club 0 03-21-2015 06:18 PM
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach Abstract The β-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly understood. With its 790 residues, BamA presents a challenge to current NMR methods. We utilized a â??divide and conquerâ?? approach in which we first obtained resonance assignments for BamAâ??s periplasmic POTRA domains 4 and 5 by solution NMR. Comparison of...
nmrlearner Journal club 0 01-08-2015 01:02 AM
Synthesis and evaluation of nitroxide-based oligoradicals for low-temperature dynamic nuclear polarization in solid state NMR
From The DNP-NMR Blog: Synthesis and evaluation of nitroxide-based oligoradicals for low-temperature dynamic nuclear polarization in solid state NMR Yau, W.-M., K.R. Thurber, and R. Tycko, Synthesis and evaluation of nitroxide-based oligoradicals for low-temperature dynamic nuclear polarization in solid state NMR. J. Magn. Reson., 2014(0). http://www.sciencedirect.com/science/article/pii/S1090780714001372
nmrlearner News from NMR blogs 0 05-28-2014 04:28 PM
[NMR paper] Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach.
Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach. Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach. Biophys J. 2013 Aug 6;105(3):699-710 Authors: Michalek M, Salnikov ES, Bechinger B Abstract The very amino-terminal domain of the huntingtin protein is directly located upstream of the protein's polyglutamine tract, plays a decisive role in several important properties of this large protein and in the development...
nmrlearner Journal club 0 08-13-2013 04:26 PM
[NMR paper] Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and
Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective. Related Articles Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective. Biophys J. 2004 Oct;87(4):2456-69 Authors: Arnold A, Paris M, Auger M Lateral diffusion is an essential process for the functioning of biological membranes. Solid-state nuclear magnetic resonance (NMR) is, a priori, a well-suited technique to study lateral diffusion within a heterogeneous...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR
Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra. Related Articles Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra. J Biomol NMR. 2003 Mar;25(3):217-23 Authors: van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H In this paper, we present a strategy for the (1)H(N) resonance assignment in solid-state magic-angle spinning (MAS) NMR, using the alpha-spectrin SH3 domain as an example. A novel 3D...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR analysis blog] Basis on qNMR: Intramolecular vs Mixtures qNMR
Basis on qNMR: Intramolecular vs Mixtures qNMR A bit of historical background NMR has won its reputation as a powerful tool for structure determination of organic molecules. In addition to the information provided by chemical shifts and coupling constants, the quantitative relationships existing between the peaks (or groups of peaks - multiplets) arising from the various nuclides in the sample has proven pivotal for the assignment and interpretation of NMR spectra. Despite the fact that the concept of quantitative NMR (qNMR) has been coupled to NMR since the early 1950, shortly...
nmrlearner News from NMR blogs 0 08-21-2010 09:12 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 02:52 PM.


Map