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 04-03-2021, 10:01 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 Probing the Interactions of Porphyrins with Macromolecules Using NMR Spectroscopy Techniques

Probing the Interactions of Porphyrins with Macromolecules Using NMR Spectroscopy Techniques

Porphyrinic compounds are widespread in nature and play key roles in biological processes such as oxygen transport in blood, enzymatic redox reactions or photosynthesis. In addition, both naturally derived as well as synthetic porphyrinic compounds are extensively explored for biomedical and technical applications such as photodynamic therapy (PDT) or photovoltaic systems, respectively. Their unique electronic structures and photophysical properties make this class of compounds so interesting...

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Conformational control of nonplanar free base porphyrins: towards bifunctional catalysts of tunable basicity #DNPNMR
From The DNP-NMR Blog: Conformational control of nonplanar free base porphyrins: towards bifunctional catalysts of tunable basicity #DNPNMR Roucan, M., M. Kielmann, S. J. Connon, S. S. R. Bernhard, and M. O. Senge. “Conformational Control of Nonplanar Free Base Porphyrins: Towards Bifunctional Catalysts of Tunable Basicity.” Chemical Communications 54, no. 1 (2018): 26–29. https://doi.org/10.1039/C7CC08099A.
nmrlearner News from NMR blogs 0 03-31-2020 04:27 AM
Trimethylsilyl tag for probing proteinâ??ligand interactions by NMR
Trimethylsilyl tag for probing proteinâ??ligand interactions by NMR Abstract Proteinâ??ligand titrations can readily be monitored with a trimethylsilyl (TMS) tag. Owing to the intensity, narrow line shape and unique chemical shift of a TMS group, dissociation constants can be determined from straightforward 1D 1H-NMR spectra not only in the fast but also in the slow exchange limit. The tag is easily attached to cysteine residues and a sensitive reporter of ligand binding also at sites where it does not interfere with ligand binding or catalytic...
nmrlearner Journal club 0 03-21-2018 04:04 PM
[NMR paper] Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy.
Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy. Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy. J Am Chem Soc. 2017 Apr 13;: Authors: Nestor G, Anderson T, Oscarson S, Gronenborn AM Abstract NMR of a uniformly (13)C-labeled carbohydrate was used to elucidate the atomic details of a sugar-protein complex. The structure of the (13)C-labeled Man?(1-2)Man?(1-2)Man?OMe trisaccharide ligand when bound...
nmrlearner Journal club 0 04-14-2017 10:27 AM
[NMR paper] Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy. Related Articles Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy. Biochim Biophys Acta. 2013 Oct 29; Authors: Pope A, Eilers M, Reeves PJ, Smith SO Abstract Rhodopsin is a classical two-state G protein-coupled receptor (GPCR). In the dark, its 11-cis retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state. Retinal-protein and protein-protein...
nmrlearner Journal club 0 11-05-2013 06:53 PM
[NMR paper] Probing the Residual Structure in Avian Prion Hexarepeats by CD, NMR and MD Techniques.
Probing the Residual Structure in Avian Prion Hexarepeats by CD, NMR and MD Techniques. Probing the Residual Structure in Avian Prion Hexarepeats by CD, NMR and MD Techniques. Molecules. 2013;18(9):11467-84 Authors: Russo L, Raiola L, Campitiello MA, Magrě A, Fattorusso R, Malgieri G, Pappalardo G, La Mendola D, Isernia C Abstract Many proteins perform essential biological functions by means of regions that lacking specific organized structure exist as an ensemble of interconverting transient conformers. The characterization of such...
nmrlearner Journal club 0 09-19-2013 02:19 PM
[NMR paper] Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules.
Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules. Acc Chem Res. 2013 Feb 7; Authors: Hong M, Schmidt-Rohr K Abstract The determination of molecular structures using solid-state NMR spectroscopy requires distance measurement through nuclear-spin dipole-dipole couplings....
nmrlearner Journal club 0 02-09-2013 12:18 AM
[NMR paper] Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy. Related Articles Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy. Adv Exp Med Biol. 1998;435:29-38 Authors: Homans SW, Field RA, Milton MJ, Probert M, Richardson JM
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Probing the structure and interactions of crystallin proteins by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the structure and interactions of crystallin proteins by NMR spectroscopy. Prog Retin Eye Res. 1999 Jul;18(4):431-62 Authors: Carver JA The lens is composed primarily of proteins, the crystallins, at high concentration whose structure and interactions are responsible for lens transparency. As there is no protein turnover in the...
nmrlearner Journal club 0 08-21-2010 04:03 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 06:12 PM.


Map