ReviewFrontiers in molecular biosciences2016
Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions.
Review in Frontiers in molecular biosciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A coarse-grained model for disordered and multi-domain proteins.Protein science : a publication of the Protein Society · 2024Article
- Molecular switching in transcription through splicing and proline-isomerization regulates stress responses in plants.Nature communications · 2024Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Single-molecule conformational dynamics of a transcription factor reveals a continuum of binding modes controlling association and dissociation.Nucleic acids research · 2021Article
- Intrinsically Disordered Proteins as Regulators of Transient Biological Processes and as Untapped Drug Targets.Molecules (Basel, Switzerland) · 2021Review
- Molecular recognition of ubiquitin and Lys63-linked diubiquitin by STAM2 UIM-SH3 dual domain: the effect of its linker length and flexibility.Scientific reports · 2019Article
- HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.Nucleic acids research · 2019Article
- Recent advances in automated protein design and its future challenges.Expert opinion on drug discovery · 2018Review
- A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.