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



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 06-10-2014, 04:49 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,399
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 Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics

Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics

Publication date: Available online 9 June 2014
Source:Food Research International

Author(s): Minyi Han , Peng Wang , Xinglian Xu , Guanghong Zhou

The changes of water mobility and fractal dimension (Df) during pork myofibrillar proteins (PMP) heat-induced gelation were investigated using low-field nuclear magnetic resonance (NMR) and image analysis, respectively. The NMR data were related to the gel microstructure which was explained as fractal dimension and pore size using principal component analysis (PCA). Distributed exponential analysis of the T2 relaxation revealed that three water components corresponding to the three water molecule states exist during the heat-induced gelation. A significant change of T2 was occurred when the temperature increased, T21 relaxation times decreased significantly from 403.70ms to 231.01ms with the temperature increasing from 50 to 70C. The fraction of T21 distributions declined from 99.27% to 77.01% as the temperature increased from 40 to 60C. Pronounced different gel network structure was observed during the myofibrillar proteins heat-induced gelation and different Df which was determined by box count method was found between all treatments although evidencing a narrow scale range (from 2.835 to 2.860). Good correlations were detected between the NMR T2 parameters and microstructural data. Overall, combined low-field NMR, image analysis and PCA provide powerful tools for elucidating the pork myofibrillar protein heat-induced gelation.







More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.
A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors. J Med Chem. 2013 Jan 30; Authors: Dal Piaz F, Vassallo A, Temraz A, Cotugno R, Belisario MA, Bifulco G, Chini MG, Pisano C, De Tommasi N, Braca A Abstract The potential of Heat Shock Protein 90 (Hsp90) as a therapeutic target...
nmrlearner Journal club 0 02-03-2013 10:19 AM
Heat management strategies for solid-state NMR of functional proteins
Heat management strategies for solid-state NMR of functional proteins September 2012 Publication year: 2012 Source:Journal of Magnetic Resonance, Volume 222</br> </br> Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled protein (or no protein) in buffer...
nmrlearner Journal club 0 02-03-2013 10:13 AM
Heat Management Strategies for Solid-state NMR of Functional Proteins
Heat Management Strategies for Solid-state NMR of Functional Proteins Publication year: 2012 Source:Journal of Magnetic Resonance</br> Daniel J. Fowler, Michael J. Harris, Lynmarie K. Thompson</br> Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled...
nmrlearner Journal club 0 07-14-2012 01:53 PM
[NMR paper] Changes in orcine muscle water characteristics during growth--an in vitro low-field N
Changes in orcine muscle water characteristics during growth--an in vitro low-field NMR relaxation study. Related Articles Changes in orcine muscle water characteristics during growth--an in vitro low-field NMR relaxation study. J Magn Reson. 2002 Aug;157(2):267-76 Authors: Bertram HC, Rasmussen M, Busk H, Oksbjerg N, Karlsson AH, Andersen HJ This study investigates the effects of developmental stage and muscle type on the mobility and distribution of water within skeletal muscles, using low-field (1)H-NMR transverse relaxation measurements in...
nmrlearner Journal club 0 11-24-2010 08:58 PM
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L. Related Articles NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L. FEBS Lett. 2010 Oct 8; Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus,...
nmrlearner Journal club 0 10-13-2010 02:18 PM
[NMR paper] NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Related Articles NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry. 1995 Jul 11;34(27):8631-41 Authors: Zhang J, Peng X, Jonas A, Jonas J The reversible cold, heat, and pressure unfolding of RNase A and RNase A--inhibitor complex were studied by 1D and 2D 1H NMR spectroscopy. The reversible pressure denaturation experiments in the pressure range from 1 bar to 5 kbar were carried out at pH 2.0 and 10 degrees C. The cold denaturation was...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. Eur J Biochem. 1991 Dec 5;202(2):339-47 Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. Eur J Biochem. 1991 Dec 5;202(2):339-47 Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
nmrlearner Journal club 0 08-21-2010 11:12 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This Thread:

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 - 2020, 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 01:50 AM.


Map