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...
Did you find this post helpful? |
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...