Phase transitions of associative biomacromolecules
Multivalent proteins and nucleic acids, collectively referred to as multivalent associative
biomacromolecules, provide the driving forces for the formation and compositional …
biomacromolecules, provide the driving forces for the formation and compositional …
Conformational dynamics of intrinsically disordered proteins regulate biomolecular condensate chemistry
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical
reactions are executed inside of biomolecular condensates formed by ultradynamic …
reactions are executed inside of biomolecular condensates formed by ultradynamic …
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 …
phenomenon underlying the formation of membraneless organelles that harbor a multitude …
Biophysical experiments and biomolecular simulations: A perfect match?
S Bottaro, K Lindorff-Larsen - Science, 2018 - science.org
A fundamental challenge in biological research is achieving an atomic-level description and
mechanistic understanding of the function of biomolecules. Techniques for biomolecular …
mechanistic understanding of the function of biomolecules. Techniques for biomolecular …
Global structure of the intrinsically disordered protein tau emerges from its local structure
The paradigmatic disordered protein tau plays an important role in neuronal function and
neurodegenerative diseases. To disentangle the factors controlling the balance between …
neurodegenerative diseases. To disentangle the factors controlling the balance between …
Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins
FE Thomasen, K Lindorff-Larsen - Biochemical Society …, 2022 - portlandpress.com
Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a
high level of structural heterogeneity and are best described by ensembles consisting of …
high level of structural heterogeneity and are best described by ensembles consisting of …
[HTML][HTML] On the potential of machine learning to examine the relationship between sequence, structure, dynamics and function of intrinsically disordered proteins
K Lindorff-Larsen, BB Kragelund - Journal of Molecular Biology, 2021 - Elsevier
Intrinsically disordered proteins (IDPs) constitute a broad set of proteins with few uniting and
many diverging properties. IDPs—and intrinsically disordered regions (IDRs) interspersed …
many diverging properties. IDPs—and intrinsically disordered regions (IDRs) interspersed …
Binding mechanisms of intrinsically disordered proteins: theory, simulation, and experiment
In recent years, protein science has been revolutionized by the discovery of intrinsically
disordered proteins (IDPs). In contrast to the classical paradigm that a given protein …
disordered proteins (IDPs). In contrast to the classical paradigm that a given protein …
Single-molecule FRET for probing nanoscale biomolecular dynamics
Single-molecule spectroscopy is a powerful method for studying the physics of molecular
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …
How does it really move? Recent progress in the investigation of protein nanosecond dynamics by NMR and simulation
Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular
motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …
motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …