ArticleProceedings of the National Academy of Sciences of the United States of America2008
Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Decoding an Amino Acid Sequence to Extract Information on Protein Folding.Molecules (Basel, Switzerland) · 2022Review
- A multi-step nucleation process determines the kinetics of prion-like domain phase separation.Nature communications · 2021Article
- Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation.The Journal of biological chemistry · 2019Article
- Frustration and folding of a TIM barrel protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- Article
- Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore-quencher pair for short distance measurements: application to polyproline peptides.Physical chemistry chemical physics : PCCP · 2015Article
- Non-native structure appears in microseconds during the folding of E. coli RNase H.Journal of molecular biology · 2015Article
- Modulation of frustration in folding by sequence permutation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Journal of molecular biology · 2014Article
- A structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.ACS chemical biology · 2014Article
- Folding of a large protein at high structural resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam.Journal of synchrotron radiation · 2013Article
- Advances in turbulent mixing techniques to study microsecond protein folding reactions.Biopolymers · 2013Article
- An X-ray transparent microfluidic platform for screening of the phase behavior of lipidic mesophases.The Analyst · 2013Article
- The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Biophysical reviews · 2013Review
- Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Journal of molecular biology · 2013Article
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5 authors.
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Abstract
The earliest kinetic folding events for (betaalpha)(8) barrels reflect the appearance of off-pathway intermediates. Continuous-flow microchannel mixing methods interfaced to small-angle x-ray scattering (SAXS), circular dichroism (CD), time-resolved Förster resonant energy transfer (trFRET), and time-resolved fluorescence anisotropy (trFLAN) have been used to directly monitor global and specific dimensional properties of the partially folded state in the microsecond time range for a representative (betaalpha)(8) barrel protein. Within 150 micros, the alpha-subunit of Trp synthase (alphaTS) experiences a global collapse and the partial formation of secondary structure. The time resolution of the folding reaction was enhanced with trFRET and trFLAN to show that, within 30 micros, a distinct and autonomous partially collapsed structure has already formed in the N-terminal and central regions but not in the C-terminal region. A distance distribution analysis of the trFRET data confirmed the presence of a heterogeneous ensemble that persists for several hundreds of microseconds. Ready access to locally folded, stable substructures may be a hallmark of repeat-module proteins and the source of early kinetic traps in these very common motifs. Their folding free-energy landscapes should be elaborated to capture this source of frustration.
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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.