[HTML][HTML] Histone tail conformations: a fuzzy affair with DNA

M Ghoneim, HA Fuchs, CA Musselman - Trends in biochemical sciences, 2021 - cell.com
The core histone tails are critical in chromatin structure and signaling. Studies over the past
several decades have provided a wealth of information on the histone tails and their …

How does it really move? Recent progress in the investigation of protein nanosecond dynamics by NMR and simulation

O Stenström, C Champion, M Lehner… - Current Opinion in …, 2022 - Elsevier
Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular
motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …

Liquid–liquid phase separation modifies the dynamic properties of intrinsically disordered proteins

S Guseva, V Schnapka, W Adamski… - Journal of the …, 2023 - ACS Publications
Liquid–liquid phase separation of flexible biomolecules has been identified as a ubiquitous
phenomenon underlying the formation of membraneless organelles that harbor a multitude …

Histone H4 tails in nucleosomes: a fuzzy interaction with DNA

SO Rabdano, MD Shannon, SA Izmailov… - Angewandte …, 2021 - Wiley Online Library
The interaction of positively charged N‐terminal histone tails with nucleosomal DNA plays
an important role in chromatin assembly and regulation, modulating their susceptibility to …

Sequence-dependent backbone dynamics of intrinsically disordered proteins

S Dey, M MacAinsh, HX Zhou - Journal of chemical theory and …, 2022 - ACS Publications
For intrinsically disordered proteins (IDPs), a pressing question is how sequence codes for
function. Dynamics serves as a crucial link, reminiscent of the role of structure in sequence …

Heterogeneous dynamics in partially disordered proteins

SI Virtanen, AM Kiirikki, KM Mikula, H Iwaï… - Physical Chemistry …, 2020 - pubs.rsc.org
Importance of disordered protein regions is increasingly recognized in biology, but their
characterization remains challenging due to the lack of suitable experimental and theoretical …

Quantitative prediction of ensemble dynamics, shapes and contact propensities of intrinsically disordered proteins

L Yu, R Brüschweiler - PLOS Computational Biology, 2022 - journals.plos.org
Intrinsically disordered proteins (IDPs) are highly dynamic systems that play an important
role in cell signaling processes and their misfunction often causes human disease. Proper …

Localized and collective motions in HET‐s (218‐289) fibrils from combined NMR relaxation and MD simulation

AA Smith, M Ernst, S Riniker, BH Meier - Angewandte Chemie, 2019 - Wiley Online Library
Nuclear magnetic resonance (NMR) relaxation data and molecular dynamics (MD)
simulations are combined to characterize the dynamics of the fungal prion HET‐s (218‐289) …

[HTML][HTML] Biomolecular dynamics in the 21st century

CL Brooks III, AD MacKerell Jr, CB Post… - Biochimica et Biophysica …, 2024 - Elsevier
The relevance of motions in biological macromolecules has been clear since the early
structural analyses of proteins by X-ray crystallography. Computer simulations have been …

Sequence-dependent correlated segments in the intrinsically disordered region of ChiZ

A Hicks, CA Escobar, TA Cross, HX Zhou - Biomolecules, 2020 - mdpi.com
How sequences of intrinsically disordered proteins (IDPs) code for their conformational
dynamics is poorly understood. Here, we combined NMR spectroscopy, small-angle X-ray …