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
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 10-12-2015, 01:41 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,776
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 Analyzing protein structures in their native environment - R & D Magazine


R & D Magazine


Analyzing protein structures in their native environment
R & D Magazine
However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), Massachusetts Institute of Technology (MIT) researchers have shown that they can analyze the structure that a yeast protein forms as it interacts with other ...



Analyzing protein structures in their native environment - R & D Magazine
More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Analyzing protein structures in their native environment - ScienceBlog.com (blog)
Analyzing protein structures in their native environment - ScienceBlog.com (blog) http://www.bionmr.com//t3.gstatic.com/images?q=tbn:ANd9GcS3yFqw5nPhavgjcwdlEXoatLxBCzbFVU4Qylvhxl5-XQzKooe6vWgVMdhVD54E1UKbE3rJUEwj ScienceBlog.com (blog) <img alt="" height="1" width="1"> Analyzing protein structures in their native environment ScienceBlog.com (blog) Until now, it has been difficult to fully characterize the different structures that proteins can take on in their natural environments. However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), MIT...
nmrlearner Online News 0 10-09-2015 03:05 AM
[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy. Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy. Acc Chem Res. 2013 Jul 5; Authors: Opella SJ Abstract One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
nmrlearner Journal club 0 07-09-2013 02:47 PM
[NMR paper] Analyzing protein-ligand interactions by dynamic NMR spectroscopy.
Analyzing protein-ligand interactions by dynamic NMR spectroscopy. Related Articles Analyzing protein-ligand interactions by dynamic NMR spectroscopy. Methods Mol Biol. 2013;1008:243-66 Authors: Mittermaier A, Meneses E Abstract Nuclear magnetic resonance (NMR) spectroscopy can provide detailed information on protein-ligand interactions that is inaccessible using other biophysical techniques. This chapter focuses on NMR-based approaches for extracting affinity and rate constants for weakly binding transient protein complexes with lifetimes...
nmrlearner Journal club 0 06-05-2013 06:53 PM
[NMR paper] Solid State NMR Strategy for Characterizing Native Membrane Protein Structures.
Solid State NMR Strategy for Characterizing Native Membrane Protein Structures. Related Articles Solid State NMR Strategy for Characterizing Native Membrane Protein Structures. Acc Chem Res. 2013 Mar 7; Authors: Murray DT, Das N, Cross TA Abstract Unlike water soluble proteins, the structures of helicaltransmembrane proteins depend on a very complex environment. These proteins sit in the midst of dramatic electrical and chemical gradients and are often subject to variations in the lateral pressure profile, order parameters, dielectric...
nmrlearner Journal club 0 03-09-2013 11:05 AM
[NMR paper] Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment. Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment. Methods Mol Biol. 2013;974:389-413 Authors: Arora A Abstract Several recent advancements have transformed solution NMR spectroscopy into a competitive, elegant, and eminently viable technique for determining the solution structures of membrane proteins at the level of atomic resolution. Once a good level of cell-based or...
nmrlearner Journal club 0 02-14-2013 02:37 PM
[NMR paper] Generation of native-like protein structures from limited NMR data, modern force fiel
Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling. Related Articles Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling. J Biomol NMR. 2005 Jan;31(1):59-64 Authors: Chen J, Won HS, Im W, Dyson HJ, Brooks CL Determining an accurate initial native-like protein fold is one of the most important and time-consuming steps of de novo NMR structure determination. Here we demonstrate that high-quality...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Dynamical characterization of residual and non-native structures in a partially folde
Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times. Related Articles Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times. Protein Sci. 2002 Apr;11(4):957-64 Authors: Ochsenbein F, Neumann JM, Guittet E, van Heijenoort C A spectral density model based on a truncated lorentzian distribution of...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data. Related Articles A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data. J Magn Reson. 1998 Feb;130(2):329-34 Authors: Daragan VA, Mayo KH A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational...
nmrlearner Journal club 0 11-17-2010 11:06 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 01:17 PM.


Map