Showing results 1 to 5 of 5
Search took 0.00 seconds.
Search:
Posts From Last Day
|
|
Thread / Thread Starter |
Last Post |
Replies |
Views |
Forum |
|
|
[NMR paper]
Detecting Bound Ions in Ion Channels by Solid-State NMR Experiments on (15)N-Labelled Ammonium Ions
Detecting Bound Ions in Ion Channels by Solid-State NMR Experiments on (15)N-Labelled Ammonium Ions
Solid-state NMR allows for the study of membrane proteins under physiological conditions. Here we describe a method for detection of bound ions in the selectivity filter of ion channels using solid-state NMR. This method employs standard ¹H-detected solid-state NMR setup and experiment types, which is enabled by using ^(15)N-labelled ammonium ions to mimic potassium ions.
More...
nmrlearner
|
|
0 |
5 |
Journal club |
|
|
[NMR paper]
Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers
Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers
Deuterium (²H) spin relaxation of ^(13)CH(2)D methyl groups has been widely applied to investigate picosecond-to-nanosecond conformational dynamics in proteins by solution-state NMR spectroscopy. The B(0) dependence of the ²H spin relaxation rates is represented by a linear relationship between the spectral density function at three discrete frequencies J(0), J(?(D)) and J(2?(D)). In this study, the linear relation between ²H relaxation rates at B(0) fields separated by a...
nmrlearner
|
|
0 |
4 |
Journal club |
|
|
[NMR paper]
Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy
Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy
The effects of two macromolecular cosolutes, specifically the polysaccharide dextran-20 and the protein lysozyme, on the aggregation kinetics of a pathogenic huntingtin exon-1 protein (hht^(ex1)) with a 35 polyglutamine repeat, htt^(ex1)Q(35), are described. A unified kinetic model that establishes a direct connection between reversible tetramerization occurring on the microsecond time scale and irreversible fibril formation on a time scale of hours/days forms the basis for...
nmrlearner
|
|
0 |
28 |
Journal club |
|
|
[NMR paper]
Cryo-EM and Solid State NMR Together Provide a More Comprehensive Structural Investigation of Protein Fibrils
Cryo-EM and Solid State NMR Together Provide a More Comprehensive Structural Investigation of Protein Fibrils
The Tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally,...
nmrlearner
|
|
0 |
13 |
Journal club |
|
|
[NMR paper]
General Characterization of Properties of Ordered and Disordered Proteins by Wide-Line (1)H NMR
General Characterization of Properties of Ordered and Disordered Proteins by Wide-Line (1)H NMR
Wide-line ¹H NMR is an efficient spectroscopic method to determine the disorder tendency of a protein. It directly measures the properties of the hydration shell of proteins, delivering exact and measurable values of their disorder/order content. A comparison is performed between several globular and disordered proteins. The common properties of the subzero mobile hydration water of these two groups were investigated. The amount of the mobile hydration water and the shape of the melting...
nmrlearner
|
|
0 |
49 |
Journal club |