Conformational dynamics of intrinsically disordered proteins regulate biomolecular condensate chemistry

A Abyzov, M Blackledge, M Zweckstetter - Chemical Reviews, 2022 - ACS Publications
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical
reactions are executed inside of biomolecular condensates formed by ultradynamic …

Structure, dynamics, assembly, and evolution of protein complexes

JA Marsh, SA Teichmann - Annual review of biochemistry, 2015 - annualreviews.org
The assembly of individual proteins into functional complexes is fundamental to nearly all
biological processes. In recent decades, many thousands of homomeric and heteromeric …

[HTML][HTML] flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions

G Hu, A Katuwawala, K Wang, Z Wu… - Nature …, 2021 - nature.com
Identification of intrinsic disorder in proteins relies in large part on computational predictors,
which demands that their accuracy should be high. Since intrinsic disorder carries out a …

Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins

L Kurgan, G Hu, K Wang, S Ghadermarzi, B Zhao… - Nature …, 2023 - nature.com
Intrinsic disorder is instrumental for a wide range of protein functions, and its analysis, using
computational predictions from primary structures, complements secondary and tertiary …

[HTML][HTML] Dynamic foldamer chemistry

BAF Le Bailly, J Clayden - Chemical Communications, 2016 - pubs.rsc.org
Foldamers can be made more than pieces of static, conformationally uniform molecular
architecture by designing into their structure the conformational dynamism characteristic of …

Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy

Y Sakiyama, A Mazur, LE Kapinos, RYH Lim - Nature nanotechnology, 2016 - nature.com
Nuclear pore complexes (NPCs) are biological nanomachines that mediate the bidirectional
traffic of macromolecules between the cytoplasm and nucleus in eukaryotic cells. This …

Molecular recognition features (MoRFs) in three domains of life

J Yan, AK Dunker, VN Uversky, L Kurgan - Molecular BioSystems, 2016 - pubs.rsc.org
Intrinsically disordered proteins and protein regions offer numerous advantages in the
context of protein–protein interactions when compared to the structured proteins and …

High-throughput prediction of RNA, DNA and protein binding regions mediated by intrinsic disorder

Z Peng, L Kurgan - Nucleic acids research, 2015 - academic.oup.com
Intrinsically disordered proteins and regions (IDPs and IDRs) lack stable 3D structure under
physiological conditions in-vitro, are common in eukaryotes, and facilitate interactions with …

Protein intrinsic disorder and structure-function continuum

VN Uversky - Progress in molecular biology and translational …, 2019 - Elsevier
The functional proteome of a given organism noticeably exceeds its corresponding genome
due to various events at the DNA (genetic variations), mRNA (alternative splicing, alternative …

Binding without folding–the biomolecular function of disordered polyelectrolyte complexes

B Schuler, A Borgia, MB Borgia, PO Heidarsson… - Current opinion in …, 2020 - Elsevier
Highlights•Highly charged intrinsically disordered proteins can form high-affinity complexes
without gain of structure or site-specific interactions.•Such highly disordered polyelectrolyte …