ArticleBiophysical journal2007
Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Comparative Analysis of Biochemical and Cellular Assay Conditions and the Need for a Buffer That Mimics Cytoplasmic Environments.Molecules (Basel, Switzerland) · 2025Review
- The Hidden Influences of Macromolecular Crowding: A New Frontier in Cellular Biology and Medicine.Sub-cellular biochemistry · 2025Review
- Pitfalls of Using ANS Dye Under Molecular Crowding Conditions.International journal of molecular sciences · 2024Article
- Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins.International journal of molecular sciences · 2023Review
- Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.The journal of physical chemistry letters · 2022Article
- Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.Plant, cell & environment · 2021Article
- Interaction of polyethylene glycol with cytochrome c investigated via in vitro and in silico approaches.Scientific reports · 2021Article
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers in molecular biosciences · 2021Article
- Liquid-Liquid Phase Separation in Crowded Environments.International journal of molecular sciences · 2020Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.Cellular and molecular life sciences : CMLS · 2018Review
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- The Differential Response of Proteins to Macromolecular Crowding.PLoS computational biology · 2016Article
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Molecular-crowding effects on single-molecule RNA folding/unfolding thermodynamics and kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.The Journal of cell biology · 2013Article
- Altered protein conformation and lower stability of the dystrophic transforming growth factor beta-induced protein mutants.Molecular vision · 2013Article
- Crowding, molecular volume and plasticity: an assessment involving crystallography, NMR and simulations.Journal of biosciences · 2012Article
- Destabilization of the outer and inner mitochondrial membranes by core and linker histones.PloS one · 2012Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
We studied the secondary structure of the C-terminal domains of the histone H1 subtypes H1 degrees (C-H1 degrees ) and H1t (C-H1t) in the presence of macromolecular crowding agents (Ficoll 70 and PEG 6000) by IR spectroscopy. The carboxyl-terminal domain has little structure in aqueous solution but became extensively folded in the presence of crowding agents. In 30% PEG, C-H1 degrees contained 19% alpha-helix, 28% beta-sheet, 16% turns, and 31% open loops. Similar proportions were observed in 30% Ficoll 70 and for C-H1t in both crowding agents. The proportions of secondary structure motifs were comparable to those of the DNA-bound domain. Kratky plots of the small-angle x-ray scattering showed that in crowding agents the C-terminus had the compaction of a globular state. Progressive dissipation of the secondary structure and a linear increase in partial heat capacity with temperature together with increased binding of ANS indicated that the C-terminus is not cooperatively folded in crowded conditions. Native-like secondary structure and compactness in absence of folding cooperativity indicate that the C-terminus in crowding agents is in a molten globule state. Folding of the C-terminus in crowded conditions may increase the rate of the transition toward the DNA-bound state and facilitate H1 diffusion inside cell nuclei.
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