ArticleProceedings of the National Academy of Sciences of the United States of America2009
Continuous dissolution of structure during the unfolding of a small protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Thermo-Chemically Modified Silk Scaffolds Reveal Niche-Driven Regulation of Hematopoiesis and Fibrosis.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics.Biophysical journal · 2024Article
- Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein.Biophysical journal · 2023Article
- Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein.Protein science : a publication of the Protein Society · 2022Article
- Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores.STAR protocols · 2022Article
- Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence.Journal of molecular biology · 2021Article
- Designed folding pathway of modular coiled-coil-based proteins.Nature communications · 2021Article
- New Insights into Folding, Misfolding, and Nonfolding Dynamics of a WW Domain.The journal of physical chemistry. B · 2020Article
- Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold.Biophysical journal · 2020Article
- Structural effects of methylglyoxal glycation, a study on the model protein MNEI.Molecular and cellular biochemistry · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Switching Protein Conformational Substates by Protonation and Mutation.The journal of physical chemistry. B · 2018Article
- Fluorescence spectroscopy for revealing mechanisms in biology: Strengths and pitfalls.Journal of biosciences · 2018Review
- Tuning the Continuum of Structural States in the Native Ensemble of a Regulatory Protein.The journal of physical chemistry letters · 2017Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Article
- Autonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases H.PloS one · 2015Article
- Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.Biophysical journal · 2013Article
- Consequences of the dynamic triple peak impact factor in Traumatic Brain Injury as Measured with Numerical Simulation.Frontiers in neurology · 2013Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unfolding kinetics of many small proteins appears to be first order, when measured by ensemble-averaging probes such as fluorescence and circular dichroism. For one such protein, monellin, it is shown here that hidden behind this deceptive simplicity is a complexity that becomes evident with the use of experimental probes that are able to discriminate between different conformations in an ensemble of structures. In this study, the unfolding of monellin has been probed by measurement of the changes in the distributions of 4 different intramolecular distances, using a multisite, time-resolved fluorescence resonance energy transfer methodology. During the course of unfolding, the protein molecules are seen to undergo slow and continuous, diffusive swelling. The swelling process can be modeled as the slow diffusive swelling of a Rouse-like chain with some additional noncovalent, intramolecular interactions. Here, we show that specific structure is lost during the swelling process gradually, and not in an all-or-none manner, during unfolding.
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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.