FIGURE 1. Analysis of proteins using in-cell NMR spectroscopy.
8/04/2014 7:46:05 AM GMT
FIGURE 1. Analysis of proteins using in-cell NMR spectroscopy. More...
Similar Threads
Thread
Thread Starter
Forum
Replies
Last Post
[NMR paper] Functional dynamics of cell surface membrane proteins
Functional dynamics of cell surface membrane proteins
Publication date: Available online 22 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Noritaka Nishida , Masanori Osawa , Koh Takeuchi , Shunsuke Imai , Pavlos Stampoulis , Yutaka Kofuku , Takumi Ueda , Ichio Shimada</br>
Cell surface receptors are integral membrane proteins that receive external stimuli, and transmit signals across plasma membranes. In the conventional view of receptor activation, ligand binding to the extracellular side of the receptor induces conformational changes,...
[NMR images] Figure 3 | Nuclear magnetic resonance (NMR) spectroscopy and protein ...
http://www.nature.com/horizon/proteinfolding/background/images/technology_f3.jpg
www.nature.com
27/06/2013 2:11:12 PM GMT
Figure 3 | Nuclear magnetic resonance (NMR) spectroscopy and protein ...
More...
nmrlearner
NMR pictures
0
06-27-2013 02:10 PM
[NMR paper] Investigation of proteins in living bacteria with in-cell NMR experiments.
Investigation of proteins in living bacteria with in-cell NMR experiments.
Related Articles Investigation of proteins in living bacteria with in-cell NMR experiments.
Top Curr Chem. 2008;273:203-14
Authors: Dötsch V
Abstract
In recent years NMR methods have been developed that enable the observation of proteins insideliving bacterial cells. Because of the sensitivity of the chemical shift to environmental changesthese in-cell NMR experiments can be used to study protein conformation, molecular interaction ordynamics in a*protein's natural...
nmrlearner
Journal club
0
04-24-2013 09:48 PM
[NMR paper] Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
Biochim Biophys Acta. 2013 Jan 26;
Authors: Rose HM, Stuiver M, Thongwichian R, Theillet FX, Feller SM, Selenko P
Abstract
We comparatively analyzed the basal activity...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Abstract Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the...
nmrlearner
Journal club
0
09-20-2012 06:06 AM
[NMR paper] Cell-free synthesis of 15N-labeled proteins for NMR studies.
Cell-free synthesis of 15N-labeled proteins for NMR studies.
Related Articles Cell-free synthesis of 15N-labeled proteins for NMR studies.
IUBMB Life. 2005 Sep;57(9):615-22
Authors: Ozawa K, Dixon NE, Otting G
Modern cell-free in vitro protein synthesis systems present powerful tools for the synthesis of isotope-labeled proteins in high yields. The production of selectively 15 N-labeled proteins from 15 N-labeled amino acids is particularly economic and yields are often sufficient to analyze the proteins very quickly by two-dimensional NMR...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes fro
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
Related Articles 19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
J Am Chem Soc. 2010 Jul 7;132(26):8822-4
Authors: Ieronimo M, Afonin S, Koch K, Berditsch M, Wadhwani P, Ulrich AS
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity...