ArticleProteins2010
On the mechanism of protein fold-switching by a molecular sensor.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- Engineering protein activity into off-the-shelf DNA devices.Cell reports methods · 2022Article
- Engineering a Fluorescent Protein Color Switch Using Entropy-Driven β-Strand Exchange.ACS sensors · 2022Article
- The Next Frontier for Designing Switchable Proteins: Rational Enhancement of Kinetics.The journal of physical chemistry. B · 2021Article
- Large enhancement of response times of a protein conformational switch by computational design.Nature communications · 2018Article
- Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Scientific reports · 2017Article
- Construction of Allosteric Protein Switches by Alternate Frame Folding and Intermolecular Fragment Exchange.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Influence of Secondary-Structure Folding on the Mutually Exclusive Folding Process of GL5/I27 Protein: Evidence from Molecular Dynamics Simulations.International journal of molecular sciences · 2016Article
- Converting a binding protein into a biosensing conformational switch using protein fragment exchange.Biochemistry · 2014Article
- Stepwise conversion of a binding protein to a fluorescent switch: application to Thermoanaerobacter tengcongensis ribose binding protein.Biochemistry · 2013Article
- Protein conformational switches: from nature to design.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Review
- Agonism/antagonism switching in allosteric ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural characterization of two alternate conformations in a calbindin D₉k-based molecular switch.Biochemistry · 2011Article
- Molecular simulations of mutually exclusive folding in a two-domain protein switch.Biophysical journal · 2011Article
- Converting a protein into a switch for biosensing and functional regulation.Protein science : a publication of the Protein Society · 2011Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Alternate frame folding (AFF) is a mechanism by which conformational change can be engineered into a protein. The protein structure switches from the wild-type fold (N) to a circularly-permuted fold (N'), or vice versa, in response to a signaling event such as ligand binding. Despite the fact that the two native states have similar structures, their interconversion involves folding and unfolding of large parts of the molecule. This rearrangement is reported by fluorescent groups whose relative proximities change as a result of the order-disorder transition. The nature of the conformational change is expected to be similar from protein to protein; thus, it may be possible to employ AFF as a general method to create optical biosensors. Toward that goal, we test basic aspects of the AFF mechanism using the AFF variant of calbindin D(9k). A simple three-state model for fold switching holds that N and N' interconvert through the unfolded state. This model predicts that the fundamental properties of the switch--calcium binding affinity, signal response (i.e., fluorescence change upon binding), and switching rate--can be controlled by altering the relative stabilities of N and N'. We find that selectively destabilizing N or N' changes the equilibrium properties of the switch (binding affinity and signal response) in accordance with the model. However, kinetic data indicate that the switching pathway does not require whole-molecule unfolding. The rate is instead limited by unfolding of a portion of the protein, possibly in concert with folding of a corresponding region.
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What OpenQuestion holds
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.