[NMR paper] Reversible DNA-protein cross-linking at epigenetic DNA marks
Reversible DNA-protein cross-linking at epigenetic DNA marks
5-Formylcytosine (5fC) is an endogenous DNA modification frequently found within regulatory elements of mammalian genes. Although 5fC is an oxidation product of 5-methylcytosine (5mC), the two epigenetic marks show distinct genome-wide distributions and protein affinities, suggesting that they perform different functions in epigenetic signaling. A unique feature of 5fC is the presence of a potentially reactive aldehyde group in its structure. Here, we show that 5fC bases in DNA readily form Schiff base conjugates with Lys side...
nmrlearner
Journal club
0
09-12-2017 01:45 PM
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcSCXR38-W1skwr6nJyTpI7ekwp0MTCyjWVm3-nHyO5fN0ai5Hxu348VoeOV77NUFQBjMN6RfXbk
Nature.com
<img alt="" height="1" width="1">
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
Nature.com
We describe an integrated workflow that robustly identifies cross-links from endogenous protein complexes in human cellular lysates. Our approach is based on the application of mass spectrometry (MS)-cleavable cross-linkers,...
nmrlearner
Online News
0
09-29-2015 07:59 AM
[NMR paper] NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
Related Articles NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
J Phys Chem B. 2015 Apr 7;
Authors: Makwana KM, Mahalakshmi R
Abstract
Interaction among the side chains of aromatic amino acids is a well-known mechanism of protein...
nmrlearner
Journal club
0
04-09-2015 03:47 AM
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10Â*Ã?). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a...
nmrlearner
Journal club
0
11-28-2014 11:37 AM
[NMR paper] Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Related Articles Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Biochim Biophys Acta. 2013 Oct 29;
Authors: Pope A, Eilers M, Reeves PJ, Smith SO
Abstract
Rhodopsin is a classical two-state G protein-coupled receptor (GPCR). In the dark, its 11-cis retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state. Retinal-protein and protein-protein...
nmrlearner
Journal club
0
11-05-2013 06:53 PM
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi102012j/aop/images/medium/bi-2010-02012j_0006.gif
Biochemistry
DOI: 10.1021/bi102012j
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/1zthtU6QJBQ
More...
nmrlearner
Journal club
0
03-09-2011 04:19 AM
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Biochemistry. 2011 Feb 16;
Authors: Mealman TD, Bagai I, Singh P, Goodlet DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM
The E. coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the...
nmrlearner
Journal club
0
02-18-2011 08:07 PM
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...
Nucleotide-amino acid ?-stacking interactions initiate photo cross-linking in RNA-protein complexes - Nature.com
Linear Mode
