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



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 05-30-2017, 01:21 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,137
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 Discovery of how amyloids bind metal ions sheds light on protein function - Phys.Org

Discovery of how amyloids bind metal ions sheds light on protein function - Phys.Org


Phys.Org


Discovery of how amyloids bind metal ions sheds light on protein function
Phys.Org
â??Even though there has been a lot of high-resolution, atomic level structural work on amyloids by solid-state NMR, people have really not studied the metal-binding aspects,â?? says professor Mei Hong. Credit: Massachusetts Institute of Technology ...


Read here
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org <img alt="" height="1" width="1"> Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress Phys.Org Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain. Credit: Wiley. A special type of small sulfur-rich protein, metallothioneins, have an extraordinary capability for ... Read here
nmrlearner Online News 0 03-24-2017 10:00 AM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcQG69FMdjaOzVdvO8fNDx9c1t6uv0SeGKAywKjRdVRRma0SZH4sGlq9-_q3JW8xkTHitn6biYqD Phys.Org <img alt="" height="1" width="1"> Light microscopy provides a deep look into protein structure - Phys.org Phys.Org Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ... and more &raquo;
nmrlearner Online News 0 01-25-2017 11:13 PM
Study Sheds Light On Structure of Alzheimer Fibrils - Scicasts (press release) (blog)
<img alt="" height="1" width="1"> Study Sheds Light On Structure of Alzheimer Fibrils Scicasts (press release) (blog) Only solid-state nuclear magnetic resonance spectroscopy (solid-state NMR) is capable of offering a view at the atomic level in this case. New developments in methods made it possible to measure a network of distances between the atoms in the protein ... Study Sheds Light On Structure of Alzheimer Fibrils - Scicasts (press release) (blog) More...
nmrlearner Online News 0 08-09-2016 02:21 AM
Selective Host-Guest Interaction between Metal Ions and Metal-Organic Frameworks using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy
From The DNP-NMR Blog: Selective Host-Guest Interaction between Metal Ions and Metal-Organic Frameworks using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy Guo, Z., et al., Selective Host-Guest Interaction between Metal Ions and Metal-Organic Frameworks using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy. Chemistry, 2014: p. n/a-n/a. http://www.ncbi.nlm.nih.gov/pubmed/25297002
nmrlearner News from NMR blogs 0 10-23-2014 05:11 AM
Research discovery: Near-complete set of templates for protein complexes ... - Phys.Org
<img alt="" height="1" width="1" /> Research discovery: Near-complete set of templates for protein complexes ... Phys.Org Such accurate computer modeling is based on â??templateâ?? structures of proteins determined by X-ray crystallography and nuclear magnetic resonance. Until now, it was believed that many years of work were required before a practically useful set of ... Research discovery: Near-complete set of templates for protein complexes ... - Phys.Org More...
nmrlearner Online News 0 06-08-2012 08:47 PM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins Publication year: 2011 Source: Journal of Magnetic Resonance, Available online 30 December 2011</br> Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br> Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
nmrlearner Journal club 0 12-31-2011 10:40 AM
[NMR paper] Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate. Related Articles Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate. J Biol Chem. 2002 Apr 5;277(14):12375-81 Authors: Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein
Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. Related Articles Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. J Magn Reson. 2000 Oct;146(2):381-4 Authors: Ma C, Opella SJ Twelve amino acid residues corresponding to an "EF-hand" calcium-binding site were added to the N-terminus of a protein, providing a specific lanthanide ion binding that weakly orients the protein in solution. A...
nmrlearner Journal club 0 11-19-2010 08:29 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 - 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 12:51 PM.


Map