BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > NMR community > Online News
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 05-01-2024, 12:40 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,227
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 Water mobility and microstructure of acidified milk model gels with added whey protein ingredients - ScienceDirect.com

Water mobility and microstructure of acidified milk model gels with added whey protein ingredients - ScienceDirect.com

Water mobility and microstructure of acidified milk model gels with added whey protein ingredients ScienceDirect.com Read here
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry
Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry Whey-protein-isolate-based composite hydrogels with encapsulated black carrot (Daucus carota) extract were prepared by heat-induced gelation. The hydrogels were blended with gum tragacanth, pectin and xanthan gum polysaccharides for modulating their properties. ¹H spin-lattice relaxation experiments were performed in a broad frequency range, from 4 kHz to 30 MHz, to obtain insight into the influence of the different polysaccharides and of the presence of black carrot on dynamical properties of... More...
nmrlearner Journal club 0 09-29-2021 12:23 PM
[NMR paper] EPR and NMR study of molecular components mobility and organization in goat milk under ultrasound treatment
EPR and NMR study of molecular components mobility and organization in goat milk under ultrasound treatment The effect of ultrasound treatment on molecular mobility and organization of the main components in raw goat milk was studied by EPR and NMR spectroscopies. NMR relaxation studies showed an increase in the spin-lattice T(1) and spin-spin T(2) relaxation times in goat milk products (cream, anhydrous fat) and change in the diffusion of proton-containing molecules during ultrasound treatment. The diffusion became more uniform and could be rather accurately approximated by one effective...
nmrlearner Journal club 0 07-27-2021 12:27 PM
Heterogeneity of Network Structures and Water Dynamics in ?-Carrageenan Gels Probed by Nanoparticle Diffusometry #DNPNMR
From The DNP-NMR Blog: Heterogeneity of Network Structures and Water Dynamics in ?-Carrageenan Gels Probed by Nanoparticle Diffusometry #DNPNMR Kort, Daan W. de, Erich Schuster, Freek J.M. Hoeben, Ryan Barnes, Meike Emondts, Henk M. Janssen, Niklas Lorén, Songi Han, Henk Van As, and John P.M. van Duynhoven. “Heterogeneity of Network Structures and Water Dynamics in ?-Carrageenan Gels Probed by Nanoparticle Diffusometry.” Langmuir 34, no. 37 (September 18, 2018): 11110–20. https://doi.org/10.1021/acs.langmuir.8b01052.
nmrlearner News from NMR blogs 0 11-25-2018 06:02 AM
TD NMR as a method to determine and characterize the water-binding capacity of whey protein microparticles
TD NMR as a method to determine and characterize the water-binding capacity of whey protein microparticles Publication date: Available online 9 October 2015 Source:Food Hydrocolloids</br> Author(s): Jorien P.C.M. Peters, Frank J. Vergeldt, Henk Van As, Hannemieke Luyten, Remko M. Boom, Atze Jan van der Goot</br> Water-binding capacity (WBC) is commonly measured with a centrifugation method in which a sample is hydrated in excess water and the pellet weight after centrifugation defines the WBC. When a dispersion is being analyzed, here containing whey...
nmrlearner Journal club 0 10-10-2015 06:11 AM
Investigation the effects of protein hydration states on the mobility water and fat in meat batters by LF-NMR technique
Investigation the effects of protein hydration states on the mobility water and fat in meat batters by LF-NMR technique Publication date: Available online 8 October 2015 Source:LWT - Food Science and Technology</br> Author(s): Jun-Hua Shao, Ya-Min Deng, Li Song, A. Batur, Na Jia, Deng-Yong Liu</br> The use of LF-NMR technique for assessing the influence of meat protein hydration states on the mobility water and fat in meat batters was investigated. Three relaxation components, T22 (50 ms), T2b and T21 (lower than 10 ms) were found in meat group and fat...
nmrlearner Journal club 0 10-09-2015 03:05 AM
Milk fraud: Proteins uncover adulteration with cheaper milk - separationsNOW.com
Milk fraud: Proteins uncover adulteration with cheaper milk - separationsNOW.com http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcTF40U0883BE-H9WwYuqsiyxWd6v-rACgPPQqfsM2Xu4KPduIc0_KIf7JCcYSP9v27JytMSTgGI separationsNOW.com <img alt="" height="1" width="1" /> Milk fraud: Proteins uncover adulteration with cheaper milk separationsNOW.com In particular, NMR and IR spectroscopy, mass spectrometry, capillary electrophoresis, ELISA and the polymerase chain reaction have been successfully employed. A further technique is 2D gel electrophoresis (2-DE) which has been reported recently...
nmrlearner Online News 0 12-02-2013 09:36 AM
[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] Stability of beta-galactosidase, a model protein drug, is related to water mobility a
Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR). Related Articles Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR). Pharm Res. 1993 Jan;10(1):103-8 Authors: Yoshioka S, Aso Y, Izutsu K, Terao T The inactivation of freeze-dried beta-galactosidase during storage was studied, focusing on the effect of water mobility as measured by the spin-lattice relaxation time, T1, of...
nmrlearner Journal club 0 08-21-2010 11:53 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 08:20 PM.


Map