ArticleThe journal of physical chemistry. B2017
Intramolecular Interactions Overcome Hydration to Drive the Collapse Transition of Gly
Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 33 citations in OpenAlex.
- Backbone interactions and secondary structures in phase separation of disordered proteins.Biochemical Society transactions · 2024Review
- Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils.Biochemistry · 2021Article
- Sequence determinants of in cell condensate morphology, dynamics, and oligomerization as measured by number and brightness analysis.Cell communication and signaling : CCS · 2021Article
- Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder.The journal of physical chemistry. B · 2020Review
- Pearl-Necklace-Like Local Ordering Drives Polypeptide Collapse.Macromolecules · 2019Article
- Improvements to the ABSINTH Force Field for Proteins Based on Experimentally Derived Amino Acid Specific Backbone Conformational Statistics.Journal of chemical theory and computation · 2019Article
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
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Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Simulations and experiments show oligo-glycines, polypeptides lacking any side chains, can collapse in water. We assess the hydration thermodynamics of this collapse by calculating the hydration free energy at each of the end points of the reaction coordinate, here taken as the end-to-end distance (r) in the chain. To examine the role of the various conformations for a given r, we study the conditional distribution, P(R
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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.