ArticleProceedings of the National Academy of Sciences of the United States of America2005
Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. 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.
- Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.Molecules (Basel, Switzerland) · 2023Review
- Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion.The journal of physical chemistry. B · 2022Article
- Quality assessment and chemical diversity of Australian propolis from Apis mellifera bees.Scientific reports · 2022Article
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.Molecules (Basel, Switzerland) · 2022Review
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.Biophysical journal · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.The journal of physical chemistry. B · 2018Article
- How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.Accounts of chemical research · 2017Article
- 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
- Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR.PloS one · 2016Article
- Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing the non-native H helix translocation in apomyoglobin folding intermediates.Biochemistry · 2014Article
- Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c.Journal of the American Chemical Society · 2014Article
- Allosteric activation of the Par-6 PDZ via a partial unfolding transition.Journal of the American Chemical Society · 2013Article
- The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments.Protein science : a publication of the Protein Society · 2013Article
- Microsecond folding dynamics of apomyoglobin at acidic pH.The journal of physical chemistry. B · 2012Article
- Consequences of stabilizing the natively disordered f helix for the folding pathway of apomyoglobin.Journal of molecular biology · 2011Article
- Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water.Journal of the American Chemical Society · 2011Article
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3 authors.
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Abstract
Hydrogen/deuterium exchange followed by trapping of the labeled species in the aprotic solvent DMSO has been used to elucidate structure in both the burst-phase molten globule-folding intermediate of apomyoglobin and in an equilibrium intermediate that models the kinetic intermediate. Precise estimates can be made of exchange times in an interrupted exchange-out experiment at pH 4 followed by analysis in DMSO solution, giving extensive sequence-specific information about the structure of the equilibrium intermediate. In addition, the use of DMSO as a solvent for NMR measurements after quench-flow pH-pulse labeling experiments gives a greatly increased data set for the elucidation of the kinetic folding pathway. Interestingly, differences are observed in some regions of apomyoglobin between the equilibrium and kinetic intermediates. These differences are quantitative rather than qualitative; that is, the overall patterns of labeling and secondary structure formation remain similar between the two species. However, local differences are observed, which probably reflect the difference in the solution conditions for the equilibrium experiment (pH 4) vs. the kinetic experiment (pH 6) and the change in the status of the stabilizing hydrogen bond between the side chains of His-24 and His-119.
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