ArticleBiophysical journal2011
Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 67 citations in OpenAlex.
- Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain.Protein science : a publication of the Protein Society · 2025Article
- Dissecting Henipavirus W proteins conformational and fibrillation properties: contribution of their N- and C-terminal constituent domains.The FEBS journal · 2025Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies.International journal of molecular sciences · 2022Article
- Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins.Biomolecules · 2022Article
- Experimental Evidence of Intrinsic Disorder and Amyloid Formation by theInternational journal of molecular sciences · 2022Article
- Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin.Science advances · 2021Article
- Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family.International journal of molecular sciences · 2021Article
- Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy.Nature nanotechnology · 2021Article
- Dynamical Behavior and Conformational Selection Mechanism of the Intrinsically Disordered Sic1 Kinase-Inhibitor Domain.Life (Basel, Switzerland) · 2020Article
- The metastable states of proteins.Protein science : a publication of the Protein Society · 2020Review
- Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Scientific reports · 2017Article
- Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum.Journal of the American Society for Mass Spectrometry · 2017Article
- Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?Journal of the American Society for Mass Spectrometry · 2017Review
- Long range recognition and selection in IDPs: the interactions of the C-terminus of p53.Scientific reports · 2016Article
- The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.Scientific reports · 2015Article
- Article
- The importance of intrinsic order in a disordered protein ligand.Biophysical journal · 2014Article
- Effect of basic cell-penetrating peptides on the structural, thermodynamic, and hydrodynamic properties of a novel drug delivery vector, ELP[V5G3A2-150].Biochemistry · 2014Article
- LptA assembles into rod-like oligomers involving disorder-to-order transitions.Journal of the American Society for Mass Spectrometry · 2013Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IDPs in their unbound state can transiently acquire secondary and tertiary structure. Describing such intrinsic structure is important to understand the transition between free and bound state, leading to supramolecular complexes with physiological interactors. IDP structure is highly dynamic and, therefore, difficult to study by conventional techniques. This work focuses on conformational analysis of the KID fragment of the Sic1 protein, an IDP with a key regulatory role in the cell-cycle of Saccharomyces cerevisiae. FT-IR spectroscopy, ESI-MS, and IM measurements are used to capture dynamic and short-lived conformational states, probing both secondary and tertiary protein structure. The results indicate that the isolated Sic1 KID retains dynamic helical structure and populates collapsed states of different compactness. A metastable, highly compact species is detected. Comparison between the fragment and the full-length protein suggests that chain length is crucial to the stabilization of compact states of this IDP. The two proteins are compared by a length-independent compaction index.
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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.