ArticleProceedings of the National Academy of Sciences of the United States of America2010
Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 58 citations in OpenAlex.
- Divergent Mechanisms of Ice Growth Inhibition by Antifreeze Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Deuteron Chemical Exchange Saturation Transfer for the Detection of Slow Motions in Rotating Solids.Frontiers in molecular biosciences · 2021Article
- Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020Review
- Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Polymer mimics of biomacromolecular antifreezes.Nature communications · 2017Review
- Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Journal of the American Chemical Society · 2017Article
- Icephobic Surfaces Induced by Interfacial Nonfrozen Water.ACS applied materials & interfaces · 2017Article
- Hexagonal ice in pure water and biological NMR samples.Journal of biomolecular NMR · 2017Article
- Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Journal of biomolecular NMR · 2017Article
- Observation of ice-like water layers at an aqueous protein surface.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing membrane protein structure using water polarization transfer solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics.Journal of the Royal Society, Interface · 2014Article
- Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.Protein science : a publication of the Protein Society · 2014Article
- Long-range protein-water dynamics in hyperactive insect antifreeze proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.Journal of biomolecular NMR · 2011Article
- Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes.The journal of physical chemistry. B · 2011Article
- Anchored clathrate waters bind antifreeze proteins to ice.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions of proteins with their hydration shell and the ice lattice in frozen solution. We applied these methods to compare solvent interaction of an ice-binding type III antifreeze protein (AFP III) and ubiquitin a non-ice-binding protein in frozen solution. We measured (1)H-(1)H cross-saturation and cross-relaxation to provide evidence for a molecular contact surface between ice and AFP III at moderate freezing temperatures of -35 °C. This phenomenon is potentially unique for AFPs because ubiquitin shows no such cross relaxation or cross saturation with ice. On the other hand, we detected liquid hydration water and strong water-AFP III and water-ubiquitin cross peaks in frozen solution using relaxation filtered (2)H and HETCOR spectra with additional (1)H-(1)H mixing. These results are consistent with the idea that ubiquitin is surrounded by a hydration shell, which separates it from the bulk ice. For AFP III, the water cross peaks indicate that only a portion of its hydration shell (i.e., at the ice-binding surface) is in contact with the ice lattice. The rest of AFP III's hydration shell behaves similarly to the hydration shell of non-ice-interacting proteins such as ubiquitin and does not freeze together with the bulk water.
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