[NMR paper] Using NMR diffusion data to validate MD models of disordered proteins: test case of N-terminal tail of histone H4
Using NMR diffusion data to validate MD models of disordered proteins: test case of N-terminal tail of histone H4
MD simulations can provide uniquely detailed models of intrinsically disordered proteins (IDPs). However, these models need careful experimental validation. The coefficient of translational diffusion D(tr), measurable by pulsed-field gradient NMR, offers a potentially useful piece of experimental information related to the compactness of the IDP's conformational ensemble. Here we investigate, both experimentally and via the MD modeling, the translational diffusion of 25-residue...
nmrlearner
Journal club
0
11-22-2023 06:46 PM
[NMR paper] Explicit models of motions to analyze NMR relaxation data in proteins
Explicit models of motions to analyze NMR relaxation data in proteins
Nuclear Magnetic Resonance (NMR) is a tool of choice to characterize molecular motions. In biological macromolecules, pico- to nanosecond motions, in particular, can be probed by nuclear spin relaxation rates, which depend on the time fluctuations of the orientations of spin interaction frames. For the past 40 years, relaxation rates have been successfully analyzed using the Model-Free (MF) approach, which makes no assumption on the nature of motions and reports on the effective amplitude and...
More...
nmrlearner
Journal club
0
10-02-2022 07:47 AM
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
Abstract
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for regulation of C-H1.0 function. Since C-H1.0 is an intrinsically disordered domain, solution NMR is an excellent approach to characterize the...
nmrlearner
Journal club
0
11-25-2018 06:02 AM
[NMR paper] A systematic case study on using NMR models for molecular replacement: p53 tetrameriz
A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisited.
Related Articles A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisited.
Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1535-40
Authors: Chen YW, Clore GM
Molecular replacement using search models derived from nuclear magnetic resonance (NMR) spectroscopy has often proved problematic. It has been known for some time that the overall differences in atomic positions (r.m.s.d.)...
Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4 - ScienceDirect.com
Linear Mode
