4ame

<table><tr><td colspan='2'>[[4ame]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Blennius_americanus Blennius americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AME FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ame FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ame OCA], [https://pdbe.org/4ame PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ame RCSB], [https://www.ebi.ac.uk/pdbsum/4ame PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ame ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Some cold water marine fishes avoid cellular damage because of freezing by expressing antifreeze proteins (AFPs) that bind to ice and inhibit its growth; one such protein is the globular type III AFP from eel pout. Despite several studies, the mechanism of ice binding remains unclear because of the difficulty in modeling the AFP-ice interaction. To further explore the mechanism, we have determined the x-ray crystallographic structure of 10 type III AFP mutants and combined that information with 7 previously determined structures to mainly analyze specific AFP-ice interactions such as hydrogen bonds. Quantitative assessment of binding was performed using a neural network with properties of the structure as input and predicted antifreeze activity as output. Using the cross-validation method, a correlation coefficient of 0.60 was obtained between measured and predicted activity, indicating successful learning and good predictive power. A large loss in the predictive power of the neural network occurred after properties related to the hydrophobic surface were left out, suggesting that van der Waal's interactions make a significant contribution to ice binding. By combining the analysis of the neural network with antifreeze activity and x-ray crystallographic structures of the mutants, we extend the existing ice-binding model to a two-step process: 1) probing of the surface for the correct ice-binding plane by hydrogen-bonding side chains and 2) attractive van der Waal's interactions between the other residues of the ice-binding surface and the ice, which increases the strength of the protein-ice interaction.

Quantitative and qualitative analysis of type III antifreeze protein structure and function.,Graether SP, DeLuca CI, Baardsnes J, Hill GA, Davies PL, Jia Z J Biol Chem. 1999 Apr 23;274(17):11842-7. PMID:10207002<ref>PMID:10207002</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Blennius americanus]]

[[Category: Baardsnes, J]]

[[Category: Davies, P L]]

[[Category: Deluca, C I]]

[[Category: Graether, S P]]

[[Category: Hill, G A]]

[[Category: Jia, Z]]

[[Category: Thermal hysteresis protein]]