Structural highlights
Function
[ANP12_ZOAAM] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth.
Publication Abstract from PubMed
The 1.8 A resolution neutron structure of deuterated type III antifreeze protein in which the methyl groups of leucine and valine residues are selectively protonated is presented. Comparison between this and the 1.85 A resolution neutron structure of perdeuterated type III antifreeze protein indicates that perdeuteration improves the visibility of solvent molecules located in close vicinity to hydrophobic residues, as cancellation effects between H atoms of the methyl groups and nearby heavy-water molecules (D2O) are avoided.
Perdeuteration: improved visualization of solvent structure in neutron macromolecular crystallography.,Fisher SJ, Blakeley MP, Howard EI, Petit-Haertlein I, Haertlein M, Mitschler A, Cousido-Siah A, Salvay AG, Popov A, Muller-Dieckmann C, Petrova T, Podjarny A Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3266-72. doi:, 10.1107/S1399004714021610. Epub 2014 Nov 28. PMID:25478844[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fisher SJ, Blakeley MP, Howard EI, Petit-Haertlein I, Haertlein M, Mitschler A, Cousido-Siah A, Salvay AG, Popov A, Muller-Dieckmann C, Petrova T, Podjarny A. Perdeuteration: improved visualization of solvent structure in neutron macromolecular crystallography. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3266-72. doi:, 10.1107/S1399004714021610. Epub 2014 Nov 28. PMID:25478844 doi:http://dx.doi.org/10.1107/S1399004714021610
