ArticleBiophysical journal2002
Dynamics of antifreeze glycoproteins in the presence of ice.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 43 citations in OpenAlex.
- Determination of the Solution Structure of Antifreeze Glycoproteins Using Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2019Article
- Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP).Beilstein journal of organic chemistry · 2019Article
- Antifreeze glycopeptides: from structure and activity studies to current approaches in chemical synthesis.Amino acids · 2017Review
- Bacterial lipoteichoic acid enhances cryosurvival.Extremophiles : life under extreme conditions · 2015Article
- Refolding of β-stranded class I chitinases of Hippophae rhamnoides enhances the antifreeze activity during cold acclimation.PloS one · 2014Article
- Thermodynamic Analysis of Thermal Hysteresis: Mechanistic Insights into Biological Antifreezes.The Journal of chemical thermodynamics · 2012Article
- Functional importance of short-range binding and long-range solvent interactions in helical antifreeze peptides.Biophysical journal · 2012Article
- Protein-ice interaction of an antifreeze protein observed with solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Calcium interacts with antifreeze proteins and chitinase from cold-acclimated winter rye.Plant physiology · 2004Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Antifreeze glycoproteins from the Greenland cod Boreogadus saida were dimethylated at the N-terminus (m*AFGP) and their dynamics and conformational properties were studied in the presence of ice using (13)C-NMR and FTIR spectroscopy. (13)C-NMR experiments of m*AFGP in D(2)O, in H(2)O, and of freeze-dried m*AFGP were performed as a function of temperature. Dynamic parameters ((1)H T(1 rho) and T(CH)) obtained by varying the contact time revealed notable differences in the motional properties of AFGP between the different states. AFGP/ice dynamics was dominated by fast-scale motions (nanosecond to picosecond time scale), suggesting that the relaxation is markedly affected by the protein hydration. The data suggest that AFGP adopts a similar type of three-dimensional fold both in the presence of ice and in the freeze-dried state. FTIR studies of the amide I band did not show a single prevailing secondary structure in the frozen state. The high number of conformers suggests a high flexibility, and possibly reflects the necessity to expose more ice-binding groups. The data suggest that the effect of hydration on the local mobility of AFGP and the lack of significant change in the backbone conformation in the frozen state may play a role in inhibiting the ice crystal growth.
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Registered trials
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.