Determination of the Solution Structure of Antifreeze Glycoproteins Using Two-Dimensional Infrared Spectroscopy.
Journal
The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034
Informations de publication
Date de publication:
07 Feb 2019
07 Feb 2019
Historique:
pubmed:
8
1
2019
medline:
15
2
2019
entrez:
8
1
2019
Statut:
ppublish
Résumé
We study the solution structure of antifreeze glycoproteins (AFGPs) with linear and two-dimensional infrared spectroscopy (2D-IR). With 2D-IR, we study the coupling between the amide I and amide II vibrations of AFGPs. The measured nonlinear spectral response constitutes a much more clearly resolved amide I spectrum than the linear absorption spectrum of the amide I vibrations and allows us to identify the different structural elements of AFGPs in solution. We find clear evidence for the presence of polyproline II (PPII) helical structures already at room temperature, and we find that the fraction of PPII structures increases when the temperature is decreased to the biological working temperature of AFGP. We observe that inhibition of the antifreeze activity of AFGP using borate buffer or enhancing the antifreeze activity using sulfate buffer does not lead to significant changes in the protein conformation. This finding indicates that AFGPs bind to ice with their sugar side chains.
Identifiants
pubmed: 30615465
doi: 10.1021/acs.jpclett.8b03468
pmc: PMC6369719
doi:
Substances chimiques
Antifreeze Proteins
0
Borates
0
Magnesium Sulfate
7487-88-9
sodium borate
91MBZ8H3QO
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
352-357Références
Biophys J. 1999 Mar;76(3):1367-76
pubmed: 10049319
Biophys J. 2000 Jun;78(6):3195-207
pubmed: 10827996
Nature. 2000 Jul 20;406(6793):322-4
pubmed: 10917536
Annu Rev Physiol. 2001;63:327-57
pubmed: 11181959
Prog Biophys Mol Biol. 2000;74(3-5):141-73
pubmed: 11226511
Biopolymers. 1975 Apr;14(4):679-94
pubmed: 1156632
Biophys J. 2002 Jan;82(1 Pt 1):464-73
pubmed: 11751333
Chem Rev. 1996 Mar 28;96(2):601-618
pubmed: 11848766
Q Rev Biophys. 2002 Nov;35(4):369-430
pubmed: 12621861
Angew Chem Int Ed Engl. 2004 Feb 6;43(7):856-62
pubmed: 14767958
J Phys Chem A. 2005 Jun 23;109(24):5303-6
pubmed: 16839053
J Phys Chem B. 2006 Sep 28;110(38):18973-80
pubmed: 16986892
J Phys Chem B. 2007 Aug 23;111(33):9993-8
pubmed: 17676791
J Am Chem Soc. 2009 Mar 11;131(9):3385-91
pubmed: 19256572
J Am Chem Soc. 2010 Sep 8;132(35):12210-1
pubmed: 20712311
J Chem Phys. 2012 Nov 14;137(18):184202
pubmed: 23163364
J Phys Chem B. 2014 Jul 17;118(28):7920-4
pubmed: 24821472
Phys Rev Lett. 2015 Jun 12;114(23):233004
pubmed: 26196799
J Phys Chem B. 2015 Nov 5;119(44):14065-75
pubmed: 26446575
J Phys Chem Lett. 2016 Dec 1;7(23):4836-4840
pubmed: 27934047
J Mol Biol. 2017 Jun 2;429(11):1705-1721
pubmed: 28454743
J Phys Chem B. 2018 Feb 15;122(6):1771-1780
pubmed: 29346730
J Am Chem Soc. 2018 Apr 11;140(14):4803-4811
pubmed: 29392937
J Phys Chem B. 2018 Jun 7;122(22):5870-5876
pubmed: 29709181
J Am Chem Soc. 2018 Aug 1;140(30):9365-9368
pubmed: 30028137
Adv Protein Chem. 1986;38:181-364
pubmed: 3541539
Int J Pept Protein Res. 1986 Oct;28(4):386-97
pubmed: 3793370
Biochem Biophys Res Commun. 1972 Jan 14;46(1):87-92
pubmed: 5006918
J Biol Chem. 1976 May 25;251(10):3033-6
pubmed: 5450
Science. 1971 Jun 11;172(3988):1152-5
pubmed: 5574522
Science. 1969 Mar 7;163(3871):1073-5
pubmed: 5764871
Biopolymers. 1984 Jul;23(7):1379-95
pubmed: 6466773
Biochim Biophys Acta. 1978 May 3;540(2):346-56
pubmed: 656475
Int J Pept Protein Res. 1981 Jan;17(1):125-9
pubmed: 7228488
Nature. 1995 Jun 1;375(6530):427-31
pubmed: 7760940
Biophys J. 1993 Sep;65(3):985-91
pubmed: 8241413
Biophys J. 1993 Jan;64(1):252-9
pubmed: 8431545