ArticleHFSP journal2008
The spectrum of biomolecular states and motions.
Article in HFSP journal, 2008. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- Mechanism of activation and the rewired network: New drug design concepts.Medicinal research reviews · 2022Review
- Rational antibody design for undruggable targets using kinetically controlled biomolecular probes.Science advances · 2021Article
- Genomic Energy Landscapes.Biophysical journal · 2017Review
- A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformers.PloS one · 2017Article
- A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.Biochemical and biophysical research communications · 2016Article
- Frustration in biomolecules.Quarterly reviews of biophysics · 2014Review
- Correlated motions and residual frustration in thrombin.The journal of physical chemistry. B · 2013Article
- Detecting repetitions and periodicities in proteins by tiling the structural space.The journal of physical chemistry. B · 2013Article
- Ensemble-based characterization of unbound and bound states on protein energy landscape.Protein science : a publication of the Protein Society · 2013Article
- Protein frustratometer: a tool to localize energetic frustration in protein molecules.Nucleic acids research · 2012Article
- On the role of frustration in the energy landscapes of allosteric proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Allostery and population shift in drug discovery.Current opinion in pharmacology · 2010Review
- Proteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape.The Journal of biological chemistry · 2010Article
- NMR spectroscopy brings invisible protein states into focus.Nature chemical biology · 2009Review
- Folding of electrostatically charged beads-on-a-string as an experimental realization of a theoretical model in polymer science.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The universe of conformational substates of a protein molecule is huge. The complete energy landscape of proteins is, therefore, complex when studied at low temperature. Many experiments under physiological conditions commonly reveal a simpler spectrum of states. These states are individually ensembles of low temperature substates. That is, room temperature experiments probe the low free energy part of the spectrum of excitations. This paper describes how the complete landscape and the spectrum of these thermally excited motions can be related to each other. On funneled landscapes, partially folded ensembles of states are the most important excited states. Their properties and their free energy spectrum can often be predicted by native topology based models. Frustration, i.e., the conflict between inconsistent stabilizing interactions that have evolved for other purposes than optimizing folding, offers another mechanism for forming low free energy excitations. Frustration can be localized and quantified using energy landscape theory. Symmetry provides an obvious route to low free energy states in oligomeric systems, where simply repositioning parts of the molecule in ways quasi-equivalent to their relation in the native structure gives nearly degenerate energies.
Identifiers
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.