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 04-27-2018, 10:26 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
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 [ASAP] Selecting for Fast Protein–Protein Association As Demonstrated on a Random TEM1 Yeast Library Binding BLIP

[ASAP] Selecting for Fast Protein–Protein Association As Demonstrated on a Random TEM1 Yeast Library Binding BLIP



Biochemistry
DOI: 10.1021/acs.biochem.8b00172



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[ASAP] Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00019/20180410/images/medium/bi-2018-00019w_0005.gif Biochemistry DOI: 10.1021/acs.biochem.8b00019 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/kty9sAc251I More...
nmrlearner Journal club 0 04-12-2018 01:01 AM
[NMR paper] Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1
Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1 Targeting PPIs with small molecules can be challenging due to large, hydrophobic binding surfaces. Here, we describe a strategy that exploits selective alpha-helical PPIs, transferring these characteristics to small molecules. The proof-of-concept is exemplified with the apoptosis regulator Mcl-1, commonly exploited by cancers to avoid cell death. Peptide directed binding uses few synthetic transformations, requires...
nmrlearner Journal club 0 07-03-2017 02:31 AM
[NMR paper] Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders. Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders. Angew Chem Int Ed Engl. 2017 Apr 07;: Authors: Wälti MA, Riek R, Orts J Abstract In early drug discovery approaches, screening hits are often weak affinity binders that are difficult to characterize in structural detail, particularly towards obtaining the 3D structure of...
nmrlearner Journal club 0 04-08-2017 10:57 AM
[NMR paper] The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence.
The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence. Related Articles The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence. Protein Pept Lett. 2016 Sep 20; Authors: Chen TC, Hsiao CL, Huang SJ, Huang JR Abstract In NMR experiments, the chemical shift is typically the first parameter measured and is a source of structural information for biomolecules. Indeed, secondary chemical shifts, the difference...
nmrlearner Journal club 0 09-23-2016 12:55 PM
[NMR paper] Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
Lipid binding protein response to a bile acid library: a combined NMR and statistical approach. Related Articles Lipid binding protein response to a bile acid library: a combined NMR and statistical approach. FEBS J. 2015 Aug 11; Authors: Tomaselli S, Pagano K, Boulton S, Zanzoni S, Melacini G, Molinari H, Ragona L Abstract Primary bile acids, differing in the hydroxylation pattern, are synthesized from cholesterol in the liver and, once formed, can undergo extensive enzyme-catalyzed glycine/taurine conjugation, giving rise to a...
nmrlearner Journal club 0 08-12-2015 10:04 PM
Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range
Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range Abstract The mechanism of signal transduction mediated by G protein-coupled receptors is a subject of intense research in pharmacological and structural biology. Ligand association to the receptor constitutes a critical event in the activation process. Solution-state NMR can be amenable to high-resolution structure determination of agonist molecules in their...
nmrlearner Journal club 0 06-25-2011 04:12 AM
[NMR paper] Insights into tyrosine phosphorylation control of protein-protein association from th
Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase. Related Articles Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 1998 Jan 20;37(3):867-77 Authors: Eisenmesser EZ, Post CB A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Related Articles Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Biochemistry. 1994 Oct 11;33(40):12032-41 Authors: Yi Q, Erman JE, Satterlee JD Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...
nmrlearner Journal club 0 08-22-2010 03:29 AM



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 10:04 PM.


Map