ArticleJournal of the American Chemical Society2009
Observation of a low-temperature, dynamically driven structural transition in a polypeptide by solid-state NMR spectroscopy.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 85 citations in OpenAlex.
- An integrated workflow for the structure elucidation of nanocrystalline powders.Communications chemistry · 2026Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- Predicted and Experimental NMR Chemical Shifts at Variable Temperatures: The Effect of Protein Conformational Dynamics.The journal of physical chemistry letters · 2024Review
- Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dynamic Nuclear Polarization Illuminates Key Protein-Lipid Interactions in the Native Bacterial Cell Envelope.Biochemistry · 2023Article
- Dynamic nuclear polarization illuminates key protein-lipid interactions in the native bacterial cell envelope.bioRxiv : the preprint server for biology · 2023Article
- Hydrogen bonding in duplex DNA probed by DNP enhanced solid-state NMR N-H bond length measurements.Frontiers in molecular biosciences · 2023Article
- DNP-enhanced solid-state NMR spectroscopy of chromatin polymers.Journal of magnetic resonance open · 2022Article
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by SpecificJournal of the American Chemical Society · 2019Article
- Heterochromatin Protein HP1α Gelation Dynamics Revealed by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2019Article
- Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Methods (San Diego, Calif.) · 2018Review
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- N,N-Diethylmethylamine as lineshape standard for NMR above 130 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected byThe journal of physical chemistry. B · 2017Article
- Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.The journal of physical chemistry. B · 2017Article
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
- Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Journal of biomolecular NMR · 2017Article
- (17)O NMR Investigation of Water Structure and Dynamics.The journal of physical chemistry. B · 2016Article
- Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.The journal of physical chemistry. B · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
At reduced temperatures, proteins and other biomolecules are generally found to exhibit dynamic as well as structural transitions. This includes a so-called protein glass transition that is universally observed in systems cooled between 200 and 230 K, and which is generally attributed to interactions between hydrating solvent molecules and protein side chains. However, there is also experimental and theoretical evidence for a low-temperature transition in the intrinsic dynamics of the protein itself, absent any solvent. Here, we use low-temperature solid-state NMR to examine site-specific fluctuations in atomic structure and dynamics in the absence of solvents. In particular, we employ magic angle spinning NMR to examine a structural phase transition associated with dynamic processes in a solvent-free polypeptide, N-f-MLF-OH, lattice at temperatures as low as 90 K. This transition is characterized by the appearance of an extra set of lines in 1D (15)N spectra as well as additional cross peaks in 2D (13)C-(13)C and (13)C-(15)N spectra. Interestingly, the gradual, temperature-dependent appearance of the new spectral component is not accompanied by the line broadening typical of dynamic transitions. A direct comparison between the spectra of N-f-MLF-OH and the analog N-f-MLF-OMe, which does not display this transition, indicates a correlation of the structural transition to the temperature dependent motion of the aromatic phenylalanine side chain. Several quantitative solid state NMR experiments were employed to provide site-specific measurements of structural and motional features of the observed transition.
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