ArticleJournal of molecular biology2013
Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Stability and cooperativity in chimeric de novo TIM barrels via quarter swapping.Protein science : a publication of the Protein Society · 2026Article
- Study on the Correlation between Functional Group Structural Parameters and Prediction of Biomass Combustion Characteristics.ACS omega · 2025Article
- Role of a high centrality residue in protein dynamics and thermal stability.Journal of structural biology · 2021Article
- A conserved folding nucleus sculpts the free energy landscape of bacterial and archaeal orthologs from a divergent TIM barrel family.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural Characterization of an ACP fromInternational journal of molecular sciences · 2020Article
- Frustration and folding of a TIM barrel protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- RheoScale: A tool to aggregate and quantify experimentally determined substitution outcomes for multiple variants at individual protein positions.Human mutation · 2018Article
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
- Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraints.Nature communications · 2017Article
- Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast.Journal of molecular biology · 2014Article
- Sequence analysis on the information of folding initiation segments in ferredoxin-like fold proteins.BMC structural biology · 2014Article
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5 authors at 1 institution in 1 country.
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Abstract
Imidazole-3-glycerol phosphate synthase is a heterodimeric allosteric enzyme that catalyzes consecutive reactions in imidazole biosynthesis through its HisF and HisH subunits. The unusually slow unfolding reaction of the isolated HisF TIM barrel domain from the thermophilic bacteria, Thermotoga maritima, enabled an NMR-based site-specific analysis of the main-chain hydrogen bonds that stabilize its native conformation. Very strong protection against exchange with solvent deuterium in the native state was found in a subset of buried positions in α-helices and pervasively in the underlying β-strands associated with a pair of large clusters of isoleucine, leucine and valine (ILV) side chains located in the α7(βα)8(βα)1-2 and α2(βα)3-6β7 segments of the (βα)8 barrel. The most densely packed region of the large cluster, α3(βα)4-6β7, correlates closely with the core of stability previously observed in computational, protein engineering and NMR dynamics studies, demonstrating a key role for this cluster in determining the thermodynamic and structural properties of the native state of HisF. When considered with the results of previous studies where ILV clusters were found to stabilize the hydrogen-bonded networks in folding intermediates for other TIM barrel proteins, it appears that clusters of branched aliphatic side chains can serve as cores of stability across the entire folding reaction coordinate of one of the most common motifs in biology.
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