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 10-10-2017, 09:37 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,777
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 Lipofuscin Formation Catalyzed by the Milk Protein ?-Lactoglobulin: Lysine Residues in Cycloretinal Synthesis

Lipofuscin Formation Catalyzed by the Milk Protein ?-Lactoglobulin: Lysine Residues in Cycloretinal Synthesis



Biochemistry
DOI: 10.1021/acs.biochem.7b00709



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR
Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR Publication date: Available online 18 September 2014 Source:Food Hydrocolloids</br> Author(s): Enamul Haque , Bhesh R. Bhandari , Michael J. Gidley , Hilton C. Deeth , Andrew K. Whittaker</br> Instability of proteins in dry form causes solubility loss of milk protein concentrate (MPC) powder upon ageing. High resolution solid state NMR techniques were used to investigate the changes in molecular structure and dynamics of proteins in MPC...
nmrlearner Journal club 0 09-19-2014 03:07 PM
[NMR paper] Rapid milk group classification by 1H NMR analysis of Le and H epitopes in human milk oligosaccharide donor samples.
Rapid milk group classification by 1H NMR analysis of Le and H epitopes in human milk oligosaccharide donor samples. Related Articles Rapid milk group classification by 1H NMR analysis of Le and H epitopes in human milk oligosaccharide donor samples. Glycobiology. 2014 Apr 29; Authors: van Leeuwen SS, Schoemaker RJ, Gerwig GJ, van Leusen-van Kan EJ, Dijkhuizen L, Kamerling JP Abstract Human milk oligosaccharides (HMOs) are a major constituent of human breast milk and play an important role in reducing the risk of infections in...
nmrlearner Journal club 0 05-03-2014 10:42 PM
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
Milk fraud: Proteins uncover adulteration with cheaper milk - spectroscopyNOW.com
Milk fraud: Proteins uncover adulteration with cheaper milk - spectroscopyNOW.com http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcTPhUrjUOyniFW8FePgJAbHPHWHY_0HkTRUZK1DeoZHstj1f_5RCgyZ0QyoxSAejg0Dp_hOaD4o spectroscopyNOW.com <img alt="" height="1" width="1" /> Milk fraud: Proteins uncover adulteration with cheaper milk spectroscopyNOW.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...
nmrlearner Online News 0 12-01-2013 09:21 PM
Lysine methylation strategies for characterizing protein conformations by NMR
Lysine methylation strategies for characterizing protein conformations by NMR Abstract In the presence of formaldehyde and a mild reducing agent, reductive methylation is known to achieve near complete dimethylation of protein amino groups under non-denaturing conditions, in aqueous media. Amino methylation of proteins is employed in mass spectrometric, crystallographic, and NMR studies. Where biosynthetic labeling is prohibitive, amino 13C-methylation provides an attractive option for monitoring folding, kinetics, proteinâ??protein and protein-DNA interactions by NMR. Here, we...
nmrlearner Journal club 0 09-10-2012 01:48 AM
Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.
Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR. Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR. Eur Phys J E Soft Matter. 2011 Feb;34(2):1-15 Authors: Fridjonsson EO, Bernin D, Seymour JD, Nydén M, Codd SL The displacement scale dependent molecular dynamics of solvent water molecules flowing through -lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different p H conditions generate structures which are characterized by magnetic...
nmrlearner Journal club 0 03-02-2011 11:54 AM
[NMR paper] N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involveme
N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Related Articles N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J. 1998 Jun 1;332 ( Pt 2):439-49 Authors: Moore GR, Cox MC, Crowe D, Osborne MJ, Rosell FI, Bujons J, Barker PD, Mauk MR, Mauk AG The reductively dimethylated derivatives of horse and yeast iso-1-ferricytochromes c have been prepared and characterized for use as NMR...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
NMR studies of the structure and environment of the milk protein alpha-lactalbumin. Related Articles NMR studies of the structure and environment of the milk protein alpha-lactalbumin. Basic Life Sci. 1990;56:231-53 Authors: Berliner LJ, Kaptein R, Koga K, Musci G
nmrlearner Journal club 0 08-21-2010 10:48 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 03:08 PM.


Map