ArticleBiochemistry2015
Fast helix formation in the B domain of protein A revealed by site-specific infrared probes.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Hydrogen-exchange behavior of the L20A mutant of the protein A B domain in guanidinium chloride: evidence for persistent native-like contacts.Scientific reports · 2026Article
- Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone, and side-chains in EL222.Protein science : a publication of the Protein Society · 2023Article
- The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium-exchange NMR spectroscopy.Protein science : a publication of the Protein Society · 2023Article
- Coupling chemical biology and vibrational spectroscopy for studies of amyloids in vitro and in cells.Current opinion in chemical biology · 2021Review
- Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery.eLife · 2019Article
- A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy.Chemical science · 2018Article
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.Biophysical journal · 2017Article
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.The journal of physical chemistry. B · 2016Article
- Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics.Biophysical journal · 2016Article
- Efficient Total Chemical Synthesis of (13) C=(18) O Isotopomers of Human Insulin for Isotope-Edited FTIR.Chembiochem : a European journal of chemical biology · 2016Article
- Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein.Journal of the American Chemical Society · 2016Article
- Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mapping fast protein folding with multiple-site fluorescent probes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
3 authors.
Funding
Abstract
Comparison of experimental and computational protein folding studies can be difficult because of differences in structural resolution. Isotope-edited infrared spectroscopy offers a direct measure of structural changes involved in protein folding at the single-residue level. Here we demonstrate the increased resolution of site-specific infrared probes to the peptide backbone in the B domain of staphylococcal protein A (BdpA). (13)C═(18)O-labeled methionine was incorporated into each of the helices using recombinant protein expression. Laser-induced temperature jumps coupled with infrared spectroscopy were used to probe changes in the peptide backbone on the submillisecond time scale. The relaxation kinetics of the buried helices, solvated helices, and labeled positions were measured independently by probing the corresponding bands assigned in the amide I region. Using these wavelength-dependent measurements, we observe a fast nanosecond phase and slower microsecond phase at each position. We find at least partial formation of helices 1-3 in the fast intermediate state that precedes the transition state. These measurements provide direct, time-resolved experimental evidence of the early formation of partial helical structure in helices 1 and 3, supporting folding models proposed by computer simulations.
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