Directly Probing the Antifreeze Protein Kinetics at the Ice/Solution Interface(<Special Issue>Crystal Growth Controlled by Macromolecules)

DOI 機関リポジトリ (HANDLE) Web Site 参考文献55件 オープンアクセス

書誌事項

タイトル別名
  • Directly probing the antifreeze protein kinetics at the ice/solution interface

この論文をさがす

説明

Antifreeze proteins (AFP) and glycoproteins (AFGP) help fish, plants, insects and bacteria survive sub-freezing environments. It is well known that these proteins function via some surface interaction, but the exact mechanism has eluded scientists. Aside from mutagenesis experiments directed towards examining the functional importance of specific residues, conclusions about the mechanism have been drawn from indirect studies or more precisely from studies that describe the proteins effects on the ice interface. Here, we will review recent work aimed at directly studying the protein kinetics at the ice interface. fluorescent microscopy is used to determine interaction planes, surface concentrations as well as adsorption characteristics, while fourier transform infra-red attenuated total reflectance (FTIR-ATR) is used to determine the protein structure vs. temperature in the liquid and solid states as well as the ice interface characteristics. Although the functions to some degree are the same, it becomes somewhat evident that the AFGP, AFP III, and spruce budworm AFP (sbwAFP) kinetics at the ice/solution interface, as well as the mechanism, can be rather different.

収録刊行物

参考文献 (55)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ