Antifreeze proteins and

Noncolligative defenses against ice formation Antifreeze proteins and glycoproteins... 

Figure 7.39. The diversity of antifreeze proteins and antifreeze glycoproteins in marine fishes. Shown are the structures of four types of AFPs (I-IV) and the AFGP found in Antarctic notothenioids and Arctic cod. AFPs I-IV are shown as ribbon structures. The tripeptide repeat (-ala-ala-thr-) and carbohydrate moiety (galactosyl-lV-acetylgalactosamine) of AFGPs illustrate the key element of AFGP structures in noto-thenioid and Arctic cod.

SELECTION FOR ICE RESISTANCE , ANTIFREEZE PROTEINS AND ICE OR HYDRATE INHIBITION... 

ADSORPTION OF ANTIFREEZE PROTEIN AND A COMMERCIAL LOW DOSAGE HYDRATE INHIBITIOR ON HYDROPHILIC AND HYDROPHOBIC SURFACES... 

We have systematically analyzed four different antifreeze proteins and their interactions with various planes of ice as well as studied their behavior in water. We have also presented our initial efforts on the dynamics of an antifreeze protein at the ice/water interface. Additionally we have discussed the... 

K.V. Ewart, B. Rubinsky, and G.L. Fletcher, Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins, Biochem. Biophys. Res. Commun., 185 (1992) 335. 

Protective and exploitive proteins Immunoglobulins Thrombin Eibrinogen Antifreeze proteins Snake and bee venom proteins Diphtheria toxin Rtcin... 

Case 2 An experimental density map for recombinant type III antifreeze protein from eel pout (AFP), which contains 66 residues and in its crystalline form is a member of the P212121 space group [20]. 

The winter flounder antifreeze protein (AFP), characterized by Sicheri and Yang [42], consists of 37 residues of eight amino acids in an a-helix configuration. The AFP protein was synthesized by the conjoining of the Aa residues determined in the glycine mold, with the exception of the two residues at each of the termini, FIOOC-Asp Thr and Ala Arg-NP and the synthesized protein fragment is left with open amidic surfaces on the... 

Antikainen M, Griffith M, Zhang J, Hon WC, Yang DSC, Pihakashi-Maunsbach K. Immunolocalization of antifreeze proteins in winter rye leaves, crowns, and roots by tissue printing. Plant Physiol 1996 110 845-857. 

The repeat sequences in solenoid proteins are often so imperfect that it is difficult to identify them without knowledge of the 3D structure or other supplementary information. In highly regular /1-solenoids, such as antifreeze proteins (Leinala et al., 2002 Liou et al., 2000) or YadA adhesin (Nummelin et al., 2004), the repeats are of the same length and sequence similarity between the repeats is discernible (so-called overt repeats). Frequently, however, the repeats in a given /1-solenoid vary in length because additional residues may be inserted at turn sites without disrupting the pattern of /1-strands that stabilizes the structure (Steinbacher et al., 1994 Yoder et al., 1993). In these cases, the structural repeats are not apparent as sequence repeats (covert repeats). 

Leinala, E. K., Davies, P. L., Doucet, D., Tyshenko, M. G., Walker, V. K., andjia, Z. (2002). A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights./. Biol. Chem. 277, 33349-33352. 

Antifreeze Protein from Fish Bloods Robert E. Feekney and Yin Yeh... 

Zeng, H. Wilson, L.D. Walker, V.K. Ripmeester, J.A. (2006a). Effect of antifreeze proteins on the nucleation, growth, and the memory effect during tetrahydrofuran clathrate hydrate formation. J. Am. Chem. Soc., 128 (9), 2844-2850. 

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