Cell-free (CF) synthesis with highly productive E. coli lysates is a convenient method to produce labeled proteins for NMR studies. Despite reduced metabolic activity in CF lysates, a certain scrambling of supplied isotope labels is still notable. Most problematic are conversions of ^(15)N labels of the amino acids L-Asp, L-Asn, L-Gln, L-Glu and L-Ala, resulting in ambiguous NMR signals as well as in label dilution. Specific inhibitor cocktails suppress most undesired conversion reactions, while...
E. coli â??Stablelabelâ?? S30 lysate for optimized cell-free NMR sample preparation
E. coli â??Stablelabelâ?? S30 lysate for optimized cell-free NMR sample preparation
Abstract
Cell-free (CF) synthesis with highly productive E. coli lysates is a convenient method to produce labeled proteins for NMR studies. Despite reduced metabolic activity in CF lysates, a certain scrambling of supplied isotope labels is still notable. Most problematic are conversions of 15N labels of the amino acids L-Asp, L-Asn, L-Gln, L-Glu and L-Ala, resulting in ambiguous NMR signals as well as in label dilution. Specific inhibitor cocktails suppress most...
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06-14-2023 10:14 PM
2nd announcement PhD position : "nonlinearities in a controlled DNP-maser" at ENS-Paris, France
From The DNP-NMR Blog:
2nd announcement PhD position : "nonlinearities in a controlled DNP-maser" at ENS-Paris, France
A PhD position is available in the NMR group of the Laboratoire des biomolécule, located in the chemistry department of the Ecole Normale Supérieure in Paris, France.
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05-11-2019 07:56 PM
[NMR paper] A "Smart" ¹²?Xe NMR Biosensor for pH-Dependent Cell Labeling.
A "Smart" ¹²?Xe NMR Biosensor for pH-Dependent Cell Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A "Smart" ¹²?Xe NMR Biosensor for pH-Dependent Cell Labeling.
J Am Chem Soc. 2015 Apr 29;137(16):5542-8
Authors: Riggle BA, Wang Y, Dmochowski IJ
Abstract
Here we present a "smart" xenon-129 NMR biosensor that undergoes a peptide conformational change and labels cells in acidic environments. To a cryptophane host molecule with high Xe...
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03-22-2016 01:46 PM
A "Smart" (129)Xe NMR Biosensor for pH-Dependent Cell Labeling
From The DNP-NMR Blog:
A "Smart" (129)Xe NMR Biosensor for pH-Dependent Cell Labeling
Riggle BA, Wang Y, Dmochowski IJ. A "Smart" (129)Xe NMR Biosensor for pH-Dependent Cell Labeling. J Am Chem Soc. 2015;137(16):5542-8.
http://www.ncbi.nlm.nih.gov/pubmed/25848822
[NMR paper] NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
J Mol Biol. 1995 Jul 7;250(2):134-43
Authors: Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D
Similar folds often occur in proteins with dissimilar sequences. The OB-fold forms a part of the structures of at least seven non-homologous proteins...
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08-22-2010 03:50 AM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...