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 11-24-2010, 09:16 PM
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 Determination of water self-diffusion coefficient in complex food products by low fie

Determination of water self-diffusion coefficient in complex food products by low field 1H PFG-NMR: comparison between the standard spin-echo sequence and the T1-weighted spin-echo sequence.

Related Articles Determination of water self-diffusion coefficient in complex food products by low field 1H PFG-NMR: comparison between the standard spin-echo sequence and the T1-weighted spin-echo sequence.

J Magn Reson. 2003 Dec;165(2):265-75

Authors: Métais A, Mariette F

In 1990, Van Den Enden et al. proposed a method for the determination of water droplet size distributions in emulsions using a pulsed-field-gradient nuclear magnetic resonance (PFG-NMR) T1-weighted stimulated-echo technique. This paper describes both the T1-weighted spin-echo sequence, an improved method based on this earlier work, and, the standard PFG spin-echo sequence. These two methods were compared for water self-diffusion coefficient measurement in the fatty protein concentrate sample used as a 'cheese model.' The transversal and longitudinal relaxation parameters T1 and T2 were determined according to the temperature and investigated for each sample; fat-free protein concentrate sample, pure anhydrous milk fat, and fatty protein concentrate sample. The water self-diffusion in fat-free protein concentrate samples followed a linear behavior. Consequently, the water self-diffusion coefficient could be easily characterized for fat-free protein concentrate samples. However, it seemed more complicated to obtain accurate water self-diffusion in fatty protein concentrate samples since the diffusion-attenuation data were fitted by a bi-exponential function. This paper demonstrates that the implementation of the T1-weighted spin-echo sequence, using the different T1 properties of water and fat phases, allows the accurate determination of water self-diffusion coefficient in a food product. To minimize the contribution of the 1H nuclei in the fat phase on the NMR echo signal, the fat protons were selectively eliminated by an additional 180 degrees pulse. This new method reduces the standard errors of diffusion data obtained with a basic spin-echo technique, by a factor of 10. The effectiveness of the use of the T1-weighted spin-echo sequence to perform accurate water self-diffusion coefficients measurement in fatty products is thus demonstrated.

PMID: 14643709 [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
[NMR paper] NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
NMR relaxation and water self-diffusion studies in whey protein solutions and gels. Related Articles NMR relaxation and water self-diffusion studies in whey protein solutions and gels. J Agric Food Chem. 2005 Aug 24;53(17):6784-90 Authors: Colsenet R, Mariette F, Cambert M The changes in water proton transverse relaxation behavior induced by aggregation of whey proteins are explained in terms of the simple molecular processes of diffusion and chemical exchange. The water self-diffusion coefficient was measured in whey protein solutions and...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by N
Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR. Related Articles Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR. J Biomol NMR. 2001 Jun;20(2):111-26 Authors: Gruschus JM, Ferretti JA Hydration site lifetimes of slowly diffusing water molecules at the protein/DNA interface of the vnd/NK-2 homeodomain DNA complex were determined using novel three-dimensional NMR techniques. The lifetimes were calculated using the ratios of ROE and NOE cross-relaxation rates between...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectrosc
Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy. Related Articles Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy. Biochemistry. 2001 Feb 20;40(7):1884-9 Authors: Rohrer M, Prisner TF, Brügmann O, Käss H, Spoerner M, Wittinghofer A, Kalbitzer HR The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dex
Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dextran hydrogels by pulsed-field-gradient NMR. Related Articles Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dextran hydrogels by pulsed-field-gradient NMR. Chem Pharm Bull (Tokyo). 1998 Nov;46(11):1836-9 Authors: Aso Y, Yoshioka S, Kojima S Crosslinked dextran hydrogels were prepared from glycidyl methacrylate (GMA)-derivatized dextran by gamma-irradiation initiation in the presence of insulin and lysozyme as model protein...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Determination of the NMR structure of the complex between U1A protein and its RNA pol
Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element. Related Articles Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element. J Biomol NMR. 1998 Jan;11(1):59-84 Authors: Howe PW, Allain FH, Varani G, Neuhaus D RNA-protein recognition is critical to post-transcriptional regulation of gene expression, yet poorly understood at the molecular level. The relatively slow progress in understanding this important area of...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by
Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy. Biochemistry. 1996 Oct 1;35(39):12694-704 Authors: Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN A tetrahedrally hydrogen-bonded structural water molecule, water 301, is seen in...
nmrlearner Journal club 0 08-22-2010 02:20 PM
[NMR paper] Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-
Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain. Related Articles Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain. J Biomol NMR. 1995 Nov;6(3):294-305 Authors: Morikawa S, Ogata K, Sekikawa A, Sarai A, Ishii S, Nishimura Y, Nakamura H The solution structure of a specific DNA complex of the minimum DNA-binding domain of the mouse c-Myb protein was determined by distance geometry calculations using a set of 1732 nuclear Overhauser enhancement...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A s
Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques. Biophys J. 1990 Nov;58(5):1183-97 Authors: Kimmich R, Gneiting T, Kotitschke K, Schnur G Experimental frequency, concentration, and...
nmrlearner Journal club 0 08-21-2010 11:04 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 08:24 PM.


Map