ArticleProceedings of the National Academy of Sciences of the United States of America2000
Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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
51 citing papers in PubMed, 170 citations in OpenAlex.
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Crystallography of Extremophile Proteins-Structural Comparisons of Psychrophilic and Hyperthermophilic Rubredoxins.Biomolecules · 2026Article
- Temperature-dependent iron motion in extremophile rubredoxins - no need for 'corresponding states'.Scientific reports · 2024Article
- Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase.International journal of molecular sciences · 2023Article
- Molecular and thermodynamic mechanisms for protein adaptation.European biophysics journal : EBJ · 2022Review
- Structure and activity of a thermally stable mutant of Acanthamoeba actophorin.Acta crystallographica. Section F, Structural biology communications · 2022Article
- The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes.Frontiers in molecular biosciences · 2022Article
- Mesophilic Pyrophosphatase Function at High Temperature: A Molecular Dynamics Simulation Study.Biophysical journal · 2020Article
- Experimental Protein Molecular Dynamics: Broadband Dielectric Spectroscopy coupled with nanoconfinement.Scientific reports · 2019Article
- POPPeT: a New Method to Predict the Protection Factor of Backbone Amide Hydrogens.Journal of the American Society for Mass Spectrometry · 2019Article
- Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cluster-Dependent Charge-Transfer Dynamics in Iron-Sulfur Proteins.Biochemistry · 2018Article
- Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- A comparative molecular dynamics study of thermophilic and mesophilic β-fructosidase enzymes.Journal of molecular modeling · 2015Article
- How amide hydrogens exchange in native proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures.Biochemistry · 2015Article
- Are coarse-grained models apt to detect protein thermal stability? The case of OPEP force field.Journal of non-crystalline solids · 2015Article
- Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.PloS one · 2015Article
- Article
- Interface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.PloS one · 2014Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rubredoxin from the hyperthermophile Pyrococcus furiosus is the most thermostable protein characterized to date with an estimated global unfolding rate of 10(-6) s(-1) at 100 degrees C. In marked contrast to these slow global dynamics, hydrogen exchange experiments here demonstrate that conformational opening for solvent access occurs in the approximately millisecond time frame or faster at 28 degrees C for all amide positions. Under these conditions all backbone amides with exchange protection factors between 10(4) and 10(6), for which EX(2) exchange kinetics were directly verified, have exchange activation energy values within 2-3 kcal/mol of that observed for unstructured peptides. The conformational flexibility of this protein is thus sufficient for water and base catalyst access to the exchanging amide with quite limited structural disruption. The common hypothesis that enhanced conformational rigidity in the folded native state underlies the increased thermal stability of hyperthermophile proteins is not supported by these data.
Indexed as
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.